SAXSdb — 9kyw

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

Scaffolding protein

OrganismNot specified

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 1–303	Not recorded	Portal protein × 2 （P26744）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 6.70 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.

Other PDB	Difference from Current Entry 9KYW	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GP8 NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN Deposited 1999-05-11	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 264–303（40 aa） Fragment：C-TERMINAL FUNCTIONAL DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.4；293 K；Pressure 1 NMR sample composition 10% WATER/90% D2O, 99.9% D2O	Resolution not provided
2GP8 NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN Deposited 1999-05-11	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 264–303（40 aa） Fragment：C-TERMINAL FUNCTIONAL DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 4.4；293 K；Pressure 1 NMR sample composition 10% WATER/90% D2O, 99.9% D2O	Resolution not provided
8I1V The asymmetric unit of P22 procapsid Deposited 2023-01-13	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric	Chain H 1–303（303 aa） Chain I 1–303（303 aa） Chain J 1–303（303 aa） Chain K 1–303（303 aa） Chain L 1–303（303 aa） Chain M 1–303（303 aa） Chain N 1–303（303 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
9KYV The scaffold dimer of phage P22 Deposited 2024-12-09	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–303（303 aa） Chain B 1–303（303 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.90 Å
9KYX The scaffold tetramer of phage P22 Deposited 2024-12-09	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 1–303（303 aa） Chain B 1–303（303 aa） Chain C 1–303（303 aa） Chain D 1–303（303 aa） Chain E 1–303（303 aa） Chain F 1–303（303 aa） Chain G 1–303（303 aa） Chain H 1–303（303 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.90 Å

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

View Construct and Data Evidence

UniProt name	VG08_BPP22
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–303； UniProt 1–303

Portal protein

OrganismNot specified

UniProt P26744

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain B； UniProt 1–725 Chain L； UniProt 1–725	Not recorded	Scaffolding protein × 1 （P26748）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 6.70 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.

Other PDB	Difference from Current Entry 9KYW	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
3LJ5 Full Length Bacteriophage P22 Portal Protein Deposited 2010-01-25	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–725（725 aa） Fragment：UNP residues 1-725 Chain B 1–725（725 aa） Fragment：UNP residues 1-725 Chain C 1–725（725 aa） Fragment：UNP residues 1-725 Chain D 1–725（725 aa） Fragment：UNP residues 1-725 Chain E 1–725（725 aa） Fragment：UNP residues 1-725 Chain F 1–725（725 aa） Fragment：UNP residues 1-725 Chain G 1–725（725 aa） Fragment：UNP residues 1-725 Chain H 1–725（725 aa） Fragment：UNP residues 1-725 Chain I 1–725（725 aa） Fragment：UNP residues 1-725 Chain J 1–725（725 aa） Fragment：UNP residues 1-725 Chain K 1–725（725 aa） Fragment：UNP residues 1-725 Chain L 1–725（725 aa） Fragment：UNP residues 1-725	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；293 K；30% tert-Butanol, 70mM sodium chloride, 2.5% PEG 400, 0.1M sodium acetate, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 7.50 Å R-free 0.263
4V4K Bacteriophage P22 Portal Protein bound to middle Tail Factor GP4. This file contain the second biological assembly Deposited 2010-04-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric	Chain M 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain N 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain O 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain P 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain Q 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain R 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain S 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain T 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain U 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain V 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain W 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain X 1–602（602 aa） Fragment：UNP RESIDUES 1-602	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；20% PEG 8000, 0.1M (NH4)2HPO4, 0.1M MES, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K	Resolution 3.25 Å R-free 0.236
4V4K Bacteriophage P22 Portal Protein bound to middle Tail Factor GP4. This file contain the second biological assembly Deposited 2010-04-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric	Chain A 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain B 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain C 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain D 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain E 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain F 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain G 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain H 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain I 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain J 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain K 1–602（602 aa） Fragment：UNP RESIDUES 1-602 Chain L 1–602（602 aa） Fragment：UNP RESIDUES 1-602	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；20% PEG 8000, 0.1M (NH4)2HPO4, 0.1M MES, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K	Resolution 3.25 Å R-free 0.236
5GAI Probabilistic Structural Models of Mature P22 Bacteriophage Portal, Hub, and Tailspike proteins Deposited 2015-12-01	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 27 PDB declaration: 27-meric	Chain A 5–725（721 aa） Chain B 5–725（721 aa） Chain C 5–725（721 aa） Chain D 5–725（721 aa） Chain E 5–725（721 aa） Chain F 5–725（721 aa） Chain G 5–725（721 aa） Chain H 5–725（721 aa） Chain I 5–725（721 aa） Chain J 5–725（721 aa） Chain W 5–725（721 aa） Chain X 5–725（721 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE；Blot for 2 seconds before plunging.	Resolution 10.50 Å
5JJ1 Structure of the Immature Procapsid Conformation of P22 Portal Protein Deposited 2016-04-22	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–602（602 aa） Fragment：UNP residues 1-602 Chain B 1–602（602 aa） Fragment：UNP residues 1-602 Chain C 1–602（602 aa） Fragment：UNP residues 1-602 Chain D 1–602（602 aa） Fragment：UNP residues 1-602 Chain E 1–602（602 aa） Fragment：UNP residues 1-602 Chain F 1–602（602 aa） Fragment：UNP residues 1-602 Chain G 1–602（602 aa） Fragment：UNP residues 1-602 Chain H 1–602（602 aa） Fragment：UNP residues 1-602 Chain I 1–602（602 aa） Fragment：UNP residues 1-602 Chain J 1–602（602 aa） Fragment：UNP residues 1-602 Chain K 1–602（602 aa） Fragment：UNP residues 1-602 Chain L 1–602（602 aa） Fragment：UNP residues 1-602	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；5% PEG 8,000, 10 mM Cesium Chloride	Resolution 3.30 Å R-free 0.315
5JJ3 Refined Structure of the Mature Virion Conformation of P22 Portal Protein Deposited 2016-04-22	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–725（725 aa） Chain B 1–725（725 aa） Chain C 1–725（725 aa） Chain D 1–725（725 aa） Chain E 1–725（725 aa） Chain F 1–725（725 aa） Chain G 1–725（725 aa） Chain H 1–725（725 aa） Chain I 1–725（725 aa） Chain J 1–725（725 aa） Chain K 1–725（725 aa） Chain L 1–725（725 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；293 K；30% tert-butanol, 70 mM sodium chloride, 2.5% PEG400 in 0.1 M sodium acetate	Resolution 7.00 Å R-free 0.260
8EAO Cryo-EM structure of the in-situ gp1-gp4 complex from bacteriophage P22 Deposited 2022-08-29	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric	Chain B 6–626（621 aa） Chain D 6–626（621 aa） Chain F 6–626（621 aa） Chain H 6–626（621 aa） Chain J 6–626（621 aa） Chain L 6–626（621 aa） Chain N 6–626（621 aa） Chain P 6–626（621 aa） Chain R 6–626（621 aa） Chain T 6–626（621 aa） Chain V 6–626（621 aa） Chain X 6–626（621 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
8TVU In situ cryo-EM structure of bacteriophage P22 portal protein: head-to-tail protein complex at 3.0A resolution Deposited 2023-08-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric	Chain A 1–725（725 aa） Chain B 1–725（725 aa） Chain D 1–725（725 aa） Chain F 1–725（725 aa） Chain H 1–725（725 aa） Chain J 1–725（725 aa） Chain L 1–725（725 aa） Chain N 1–725（725 aa） Chain P 1–725（725 aa） Chain R 1–725（725 aa） Chain T 1–725（725 aa） Chain W 1–725（725 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 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 conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain a 1–725（725 aa） Chain b 1–725（725 aa） Chain c 1–725（725 aa） Chain d 1–725（725 aa） Chain e 1–725（725 aa） Chain f 1–725（725 aa） Chain g 1–725（725 aa） Chain h 1–725（725 aa） Chain i 1–725（725 aa） Chain j 1–725（725 aa） Chain k 1–725（725 aa） Chain l 1–725（725 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 conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 58 PDB declaration: 58-meric	Chain a 1–725（725 aa） Chain b 1–725（725 aa） Chain c 1–725（725 aa） Chain d 1–725（725 aa） Chain e 1–725（725 aa） Chain f 1–725（725 aa） Chain g 1–725（725 aa） Chain h 1–725（725 aa） Chain i 1–725（725 aa） Chain j 1–725（725 aa） Chain k 1–725（725 aa） Chain l 1–725（725 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
9PDP In situ cryoEM structure of bacteriophage P22 portal barrel Deposited 2025-06-30	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: 12-meric	Chain A 602–710（109 aa） Chain B 602–710（109 aa） Chain C 602–710（109 aa） Chain D 602–710（109 aa） Chain E 602–710（109 aa） Chain F 602–710（109 aa） Chain G 602–710（109 aa） Chain H 602–710（109 aa） Chain I 602–710（109 aa） Chain J 602–710（109 aa） Chain K 602–710（109 aa） Chain L 602–710（109 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.83 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 conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 39 PDB declaration: 39-meric	Chain Bb 1–725（725 aa） Chain Bd 1–725（725 aa） Chain Bf 1–725（725 aa） Chain Bh 1–725（725 aa） Chain Bj 1–725（725 aa） Chain Bl 1–725（725 aa） Chain Bn 1–725（725 aa） Chain Bp 1–725（725 aa） Chain Br 1–725（725 aa） Chain Bt 1–725（725 aa） Chain Bv 1–725（725 aa） Chain Bx 1–725（725 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

11 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PORTL_BPP22
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–725； UniProt 1–725 Author chain L； PDBConstruct 1–725； UniProt 1–725

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	9kyw
Deposition date deposition_date	2024-12-09
Structure title title	The scaffold C-loop of phage P22
Keywords keywords	Complex, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	39.23 Å
Radius of gyration Rg (electron density) rg_electron	39.80 Å
Forward intensity I(0) i0	320523000.00
Molecular weight molecular_weight	142790.0 kDa
Excluded volume excluded_volume	177910 Å³
Envelope volume envelope_volume	250920 Å³
Hydration-shell volume shell_volume	55389 Å³
Envelope diameter envelope_diameter	164.2 Å
Shell Rg shell_rg	42.54 Å
Envelope Rg envelope_rg	40.52 Å
Shape Rg shape_rg	39.86 Å
Total Rg total_rg	39.77 Å
Total atoms total_atoms	10050
Residues n_residues	1244
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	153.2 Å
Rg (real space) rg_real	39.59 Å
Rg uncertainty (real space) rg_real_error	1.95 Å
I(0) (real space) i0_real	3.2050e+08
I(0) uncertainty (real space) i0_real_error	6.7840e+06
Rg (reciprocal space) rg_reciprocal	39.36 Å
I(0) (reciprocal space) i0_reciprocal	320400000.0000
Solution quality estimate total_estimate	0.7868
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	42.1 Å
Skewness Skewness skewness	0.695
Kurtosis Kurtosis kurtosis	0.608
Angular range angular_range	— – 0.2000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	35480000.0000
Real-space data points n_real_points	41
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.488; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.837; Smooth: 0.925

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	Scaffolding protein
Molecular weight formula_weight	33793.8 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	10050

MEPTTEIQATEDLTLSGDHAAASADSLVVDNANDNAGQEEGFEIVLKDDETAPKQDPAKNAEFARRRIERKRQRELEQQMEAVKRGELPESLRVNPDLPPQPDINAYLSEEGLAKYDYDNSRALAAFNAANTEWLMKRQDARSNAELEQQMETVKRTQQSAQYVEAARKHYDAAEKLNIPDYQEKEDAFMQLVPPAVGADIMRLFPEKSAALMYHLGANPEKARQLLAMDGQSALIELTRLSERLTLKPRGKQISSAPPADQPITGDVSAANKDAIRKQMDAAASKGDVETYRKLKAKLKGIR

Entity 2 Entity 2 polymer

Description description	Portal protein
Molecular weight formula_weight	82829.4 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,L

MADNENRLESILSRFDADWTASDEARREAKNDLFFSRVSQWDDWLSQYTTLQYRGQFDVVRPVVRKLVSEMRQNPIDVLYRPKDGARPDAADVLMGMYRTDMRHNTAKIAVNIAVREQIEAGVGAWRLVTDYEDQSPTSNNQVIRREPIHSACSHVIWDSNSKLMDKSDARHCTVIHSMSQNGWEDFAEKYDLDADDIPSFQNPNDWVFPWLTQDTIQIAEFYEVVEKKETAFIYQDPVTGEPVSYFKRDIKDVIDDLADSGFIKIAERQIKRRRVYKSIITCTAVLKDKQLIAGEHIPIVPVFGEWGFVEDKEVYEGVVRLTKDGQRLRNMIMSFNADIVARTPKKKPFFWPEQIAGFEHMYDGNDDYPYYLLNRTDENSGDLPTQPLAYYENPEVPQANAYMLEAATSAVKEVATLGVDTEAVNGGQVAFDTVNQLNMRADLETYVFQDNLATAMRRDGEIYQSIVNDIYDVPRNVTITLEDGSEKDVQLMAEVVDLATGEKQVLNDIRGRYECYTDVGPSFQSMKQQNRAEILELLGKTPQGTPEYQLLLLQYFTLLDGKGVEMMRDYANKQLIQMGVKKPETPEEQQWLVEAQQAKQGQQDPAMVQAQGVLLQGQAELAKAQNQTLSLQIDAAKVEAQNQLNAARIAEIFNNMDLSKQSEFREFLKTVASFQQDRSEDARANAELLLKGDEQTHKQRMDIANILQSQRQNQPSGSVAETPQ

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 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	—

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

Resolution resolution	6.700 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	6.70 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	21884

fit	/app/data/saxs_computation/ky/9kyw/9kyw.fit
pddf	/app/data/pr_computation/ky/9kyw/9kyw.pr.out
profile	/app/data/saxs_computation/ky/9kyw/9kyw.dat

The scaffold C-loop of phage P22

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

Scaffolding protein

State in the Current Structure

Other States of the Same Protein in the Database

Portal 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

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)