SAXSdb — 2m5s

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

Coat protein

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 223–345	Fragment：;This domain has previously been called the 'extra-density domain' and 'telokin-like domain' in the literature based on cryo-EM models ;	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 6；310.15 K；Ionic strength (raw mmCIF value) 20；Pressure ambient NMR sample composition：1.5 mM [U-100% 13C; U-100% 15N] protein, 20 mM sodium phosphate, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：1.5 mM [U-100% 13C; U-100% 15N] protein, 20 mM sodium phosphate, 1% H2O/99% D2O \| 1% H2O/99% D2O	Resolution not provided

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 2M5S	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3IYH P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 360 PDB declaration: 360-MERIC	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions blot 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 8.20 Å
3IYH P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions blot 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 8.20 Å
3IYH P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 30 PDB declaration: 30-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions blot 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 8.20 Å
3IYH P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 36 PDB declaration: 36-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions blot 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 8.20 Å
3IYH P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions blot 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 8.20 Å
3IYI P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 420 PDB declaration: 420-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions Blot for 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 9.10 Å
3IYI P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions Blot for 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 9.10 Å
3IYI P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 35 PDB declaration: 35-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions Blot for 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 9.10 Å
3IYI P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 42 PDB declaration: 42-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions Blot for 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 9.10 Å
3IYI P22 expanded head coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links Deposited 2009-12-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer 20 mM sodium phosphate buffer, pH = 7.6；pH 7.6；20 mM sodium phosphate buffer, pH = 7.6 cryo-EM vitrification conditions Blot for 2-3 seconds before plunging；89 K；Cryogen ETHANE	Resolution 9.10 Å
5UU5 Bacteriophage P22 mature virion capsid protein Deposited 2017-02-16	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 420 PDB declaration: 420-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；50 mM Tris, pH 7.6, 1 mM MgCl2, 25 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE；single blot, one second duration	Resolution 3.30 Å
5UU5 Bacteriophage P22 mature virion capsid protein Deposited 2017-02-16	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；50 mM Tris, pH 7.6, 1 mM MgCl2, 25 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE；single blot, one second duration	Resolution 3.30 Å
5UU5 Bacteriophage P22 mature virion capsid protein Deposited 2017-02-16	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 35 PDB declaration: 35-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；50 mM Tris, pH 7.6, 1 mM MgCl2, 25 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE；single blot, one second duration	Resolution 3.30 Å
5UU5 Bacteriophage P22 mature virion capsid protein Deposited 2017-02-16	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 42 PDB declaration: 42-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；50 mM Tris, pH 7.6, 1 mM MgCl2, 25 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE；single blot, one second duration	Resolution 3.30 Å
5UU5 Bacteriophage P22 mature virion capsid protein Deposited 2017-02-16	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6；50 mM Tris, pH 7.6, 1 mM MgCl2, 25 mM NaCl cryo-EM vitrification conditions Cryogen ETHANE；single blot, one second duration	Resolution 3.30 Å
8GN5 Designed pH-responsive P22 VLP Deposited 2022-08-23	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 4–428（425 aa） Chain B 4–428（425 aa） Chain C 4–428（425 aa） Chain D 4–428（425 aa）	Mutation：S43H, E54H, E153H, N287H Mutation：S43H, E54H, E153H, N287H Mutation：S43H, E54H, E153H, N287H Mutation：S43H, E54H, E153H, N287H	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；PBS buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.02 Å
8I1T The asymmetric unit of P22 empty capsid Deposited 2023-01-13	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.80 Å
8I1V The asymmetric unit of P22 procapsid Deposited 2023-01-13	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å
8U10 In situ cryo-EM structure of bacteriophage P22 gp1:gp4:gp5:gp10:gp9 N-term complex in conformation 1 at 3.2A resolution Deposited 2023-08-30	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa） Chain H 1–430（430 aa） Chain I 1–430（430 aa） Chain J 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8U11 In situ cryo-EM structure of bacteriophage P22 gp1:gp5:gp4: gp10: gp9 N-term complex in conformation 2 at 3.1A resolution Deposited 2023-08-30	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain A 1–430（430 aa） Chain B 1–430（430 aa） Chain C 1–430（430 aa） Chain D 1–430（430 aa） Chain E 1–430（430 aa） Chain F 1–430（430 aa） Chain G 1–430（430 aa） Chain H 1–430（430 aa） Chain I 1–430（430 aa） Chain J 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
9PGG Cryo-EM structure of bacteriophage P22 gp1-gp5-gp4 complex at 2.76 angstrom Deposited 2025-07-07	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 39 PDB declaration: 39-meric	Chain Aa 1–430（430 aa） Chain Ab 1–430（430 aa） Chain Ac 1–430（430 aa） Chain Ad 1–430（430 aa） Chain Ae 1–430（430 aa） Chain Af 1–430（430 aa） Chain Ag 1–430（430 aa） Chain Ah 1–430（430 aa） Chain Ai 1–430（430 aa） Chain Aj 1–430（430 aa） Chain Ak 1–430（430 aa） Chain Al 1–430（430 aa） Chain Am 1–430（430 aa） Chain An 1–430（430 aa） Chain Ao 1–430（430 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.76 Å

9 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	VG05_BPP22
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 8–130； UniProt 223–345

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	2m5s
Deposition date deposition_date	2013-03-05
Structure title title	High-resolution NMR structure and cryo-EM imaging support multiple functional roles for the accessory I-domain of phage P22 coat protein
Keywords keywords	telokin-like domain, extra-density domain, D-loop, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	15.16 Å
Radius of gyration Rg (electron density) rg_electron	14.93 Å
Forward intensity I(0) i0	2158750000.00
Molecular weight molecular_weight	390740.0 kDa
Excluded volume excluded_volume	487730 Å³
Envelope volume envelope_volume	34898 Å³
Hydration-shell volume shell_volume	16489 Å³
Envelope diameter envelope_diameter	66.1 Å
Shell Rg shell_rg	23.89 Å
Envelope Rg envelope_rg	18.70 Å
Shape Rg shape_rg	14.91 Å
Total Rg total_rg	15.14 Å
Total atoms total_atoms	55080
Residues n_residues	3720
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	54.6 Å
Rg (real space) rg_real	15.14 Å
Rg uncertainty (real space) rg_real_error	0.43 Å
I(0) (real space) i0_real	2.1590e+09
I(0) uncertainty (real space) i0_real_error	2.5910e+07
Rg (reciprocal space) rg_reciprocal	15.15 Å
I(0) (reciprocal space) i0_reciprocal	2159000000.0000
Solution quality estimate total_estimate	0.7727
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	18.0 Å
Skewness Skewness skewness	0.305
Kurtosis Kurtosis kurtosis	-0.224
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	313400.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.708; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.916; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	2m5sA00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily	240 —

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8. Citations (1)

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Description description	Coat protein
Molecular weight formula_weight	13865.6 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	55080

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

fit	/app/data/saxs_computation/m5/2m5s/2m5s.fit
pddf	/app/data/pr_computation/m5/2m5s/2m5s.pr.out
profile	/app/data/saxs_computation/m5/2m5s/2m5s.dat

High-resolution NMR structure and cryo-EM imaging support multiple functional roles for the accessory I-domain of phage P22 coat protein

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

Coat protein

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)