SAXSdb — 4zxq

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

Tail needle protein gp26

Enterobacteria phage P22

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 1–140 Chain B； UniProt 1–140 Chain C； UniProt 1–140	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 3.9；293 K；20% PEG 8000, 0.05 M Potassium phosphate monobasic pH 3.9	Resolution 2.75 Å R-free 0.252
2	Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain D； UniProt 1–140 Chain E； UniProt 1–140 Chain F； UniProt 1–140	Not recorded	CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 3.9；293 K；20% PEG 8000, 0.05 M Potassium phosphate monobasic pH 3.9	Resolution 2.75 Å R-free 0.252

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 4ZXQ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3C9I Structure of P22 Tail-Needle GP26 Bound to Xenon Gas Deposited 2008-02-15	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–233（233 aa） Chain B 1–233（233 aa） Chain C 1–233（233 aa）	Mutation：L222M Mutation：L222M Mutation：L222M	XE XENON × 7 CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；298 K；18% PEG 4000, 0.1M Ammonium Sulfate, 0.1M Ammonium Acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K, pH 4.60	Resolution 1.95 Å R-free 0.269
3C9I Structure of P22 Tail-Needle GP26 Bound to Xenon Gas Deposited 2008-02-15	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain D 1–233（233 aa） Chain E 1–233（233 aa） Chain F 1–233（233 aa）	Mutation：L222M Mutation：L222M Mutation：L222M	XE XENON × 7 CA CALCIUM ION × 1 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；298 K；18% PEG 4000, 0.1M Ammonium Sulfate, 0.1M Ammonium Acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K, pH 4.60	Resolution 1.95 Å R-free 0.269
4ZKP P22 Tail Needle Gp26 crystallized at pH 7.0 Deposited 2015-04-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–233（233 aa）	Mutation：L222M	CA CALCIUM ION × 3 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；40% PEG 1000, 0.1M MOPS pH7.0	Resolution 2.10 Å R-free 0.189
4ZKP P22 Tail Needle Gp26 crystallized at pH 7.0 Deposited 2015-04-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain B 1–233（233 aa）	Mutation：L222M	CA CALCIUM ION × 3 CL CHLORIDE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；40% PEG 1000, 0.1M MOPS pH7.0	Resolution 2.10 Å R-free 0.189
4ZKU P22 Tail Needle Gp26 crystallized at pH 10.0 Deposited 2015-04-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–233（233 aa）	Mutation：L222M	CL CHLORIDE ION × 3 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；293 K；40% PEG 4000, 0.1M CAPS pH 10.0	Resolution 2.50 Å R-free 0.225
4ZKU P22 Tail Needle Gp26 crystallized at pH 10.0 Deposited 2015-04-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain B 1–233（233 aa）	Mutation：L222M	CL CHLORIDE ION × 3 CA CALCIUM ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 10；293 K；40% PEG 4000, 0.1M CAPS pH 10.0	Resolution 2.50 Å R-free 0.225
8EAP Cryo-EM structure of the in-situ gp10-gp26 from bacteriophage P22 Deposited 2022-08-29	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain A 3–64（62 aa） Chain B 3–64（62 aa） Chain C 3–64（62 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å

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

View Construct and Data Evidence

UniProt name	NEEDL_BPP22
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–144； UniProt 1–140 Author chain B； PDBConstruct 5–144； UniProt 1–140 Author chain C； PDBConstruct 5–144； UniProt 1–140 Author chain D； PDBConstruct 5–144； UniProt 1–140 Author chain E； PDBConstruct 5–144； UniProt 1–140 Author chain F； PDBConstruct 5–144； UniProt 1–140

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	4zxq
Deposition date deposition_date	2015-05-20
Structure title title	P22 Tail Needle Gp26 1-140 crystallized at pH 3.9
Keywords keywords	Viral protein, P22, Tail Needle, Membrane penetration; VIRAL PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	51.57 Å
Radius of gyration Rg (electron density) rg_electron	53.08 Å
Forward intensity I(0) i0	131289000.00
Molecular weight molecular_weight	89933.0 kDa
Excluded volume excluded_volume	110930 Å³
Envelope volume envelope_volume	167610 Å³
Hydration-shell volume shell_volume	29954 Å³
Envelope diameter envelope_diameter	194.5 Å
Shell Rg shell_rg	46.43 Å
Envelope Rg envelope_rg	53.10 Å
Shape Rg shape_rg	53.14 Å
Total Rg total_rg	52.63 Å
Total atoms total_atoms	6321
Residues n_residues	840
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	185.7 Å
Rg (real space) rg_real	52.21 Å
Rg uncertainty (real space) rg_real_error	3.86 Å
I(0) (real space) i0_real	1.3130e+08
I(0) uncertainty (real space) i0_real_error	3.0190e+06
Rg (reciprocal space) rg_reciprocal	51.03 Å
I(0) (reciprocal space) i0_reciprocal	131100000.0000
Solution quality estimate total_estimate	0.7541
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	53.9 Å
Skewness Skewness skewness	0.568
Kurtosis Kurtosis kurtosis	-0.301
Angular range angular_range	— – 0.1550 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3563000.0000
Real-space data points n_real_points	32
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.629; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.473; Smooth: 0.443

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Tail needle protein gp26
Molecular weight formula_weight	15306.8 kDa
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F
Atom count atom_count	6816

GPGSMADPSLNNPVVIQATRLDASILPRNVFSKSYLLYVIAQGTDVGAIAGKANEAGQGAYDAQVKNDEQDVELADHEARIKQLRIDVDDHESRITANTKAITALNVRVTTAEGEIASLQTNVSALDGRVTTAENNISALQADY

来源 Source

来源生物 organism	Enterobacteria phage P22
NCBI Class编号 ncbi_taxonomy_id	10754
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	495

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8. Citations (1)

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Unit-cell length a length_a	58.952 Å
Unit-cell length b length_b	94.095 Å
Unit-cell length c length_c	97.619 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	12

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.750 Å
Low-resolution limit resolution_low	15.862 Å
R factor r_factor	0.2167
R_work r_work	0.2149
R_free r_free	0.2518

fit	/app/data/saxs_computation/zx/4zxq/4zxq.fit
pddf	/app/data/pr_computation/zx/4zxq/4zxq.pr.out
profile	/app/data/saxs_computation/zx/4zxq/4zxq.dat

P22 Tail Needle Gp26 1-140 crystallized at pH 3.9

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

Tail needle protein gp26

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

Diffraction experiment Diffraction