SAXSdb — 9ky2

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

Beta-arrestin-2

Bos taurus

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain A； UniProt 1–420 Chain F； UniProt 1–420	Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	Fab30 Heavy Chain × 2 Fab30 Light Chain × 2 C5a anaphylatoxin chemotactic receptor 1 × 2 （P30993）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.78 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 9KY2	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5TV1 active arrestin-3 with inositol hexakisphosphate Deposited 2016-11-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 8–393（386 aa） Fragment：UNP residues 8-393	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 6 GOL GLYCEROL × 9	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；100 mM Succinate/Phosphate/Glycine pH 8.5 and 25% PEG 1500	Resolution 2.40 Å R-free 0.245
8GO9 Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human Atypical chemokine receptor 2, ACKR2 (D6R) Deposited 2022-08-24	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–420（420 aa） Chain F 1–420（420 aa）	Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Blotted for 3 seconds before plunging.	Resolution 3.35 Å
8GOC Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human Vasopressin V2 receptor, V2R Deposited 2022-08-24	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–420（420 aa） Chain B 1–420（420 aa） Chain C 1–420（420 aa）	Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Blotted for 3 seconds before plunging.	Resolution 4.18 Å
8GOO Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human C5a anaphylatoxin chemotactic receptor 1, C5aR1 Deposited 2022-08-25	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–420（420 aa） Chain B 1–420（420 aa） Chain C 1–420（420 aa）	Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C66V,L69C,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Blotted for 3 seconds before plunging.	Resolution 4.40 Å
8I0Z Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human C5a anaphylatoxin chemotactic receptor 1, C5aR1 (Local refine) Deposited 2023-01-12	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–420（420 aa） Chain B 1–420（420 aa） Chain C 1–420（420 aa）	Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Blotted for 3 seconds before plunging.	Resolution 4.33 Å
8I10 Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human Vasopressin V2 receptor, V2R (Local refine) Deposited 2023-01-12	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–420（420 aa） Chain B 1–420（420 aa） Chain C 1–420（420 aa）	Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Blotted for 3 seconds before plunging.	Resolution 3.96 Å
8J8R Structure of beta-arrestin2 in complex with M2Rpp Deposited 2023-05-02	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric	Chain A 1–420（420 aa） Chain B 1–420（420 aa） Chain C 1–420（420 aa）	Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
8J8V Structure of beta-arrestin2 in complex with D6Rpp (Local Refine) Deposited 2023-05-02	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–420（420 aa） Chain F 1–420（420 aa）	Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A Mutation：C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Blotted for 3 seconds before plunging.	Resolution 3.22 Å
8TIL Human ACKR3 phosphorylated by GRK5 in complex with Arrestin3 reconstructed without receptor/micelle Deposited 2023-07-19	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–392（392 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
8TIN Human ACKR3 phosphorylated by GRK2 in complex with Arrestin3 reconstructed without receptor/micelle Deposited 2023-07-19	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–392（392 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.00 Å
8VJ9 CryoEM structure of human ACKR3 phosphorylated by GRK5 in complex with Arrestin3 variant with the C edge loop from Arrestin2 inserted Deposited 2024-01-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–392（392 aa） Fragment：Arrestin3 variant with the C edge loop from Arrestin2 inserted	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å

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

View Construct and Data Evidence

UniProt name	ARRB2_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–420； UniProt 1–420 Author chain F； PDBConstruct 1–420； UniProt 1–420

C5a anaphylatoxin chemotactic receptor 1

OrganismNot specified

UniProt P30993

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain U； UniProt 329–351 Chain V； UniProt 329–351	Non-standard monomer：Yes (specific site not provided by mmCIF)	Beta-arrestin-2 × 2 （P32120） Fab30 Heavy Chain × 2 Fab30 Light Chain × 2	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.78 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 9KY2	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8HPT Structure of C5a-pep bound mouse C5aR1 in complex with Go Deposited 2022-12-13	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 2–351（350 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.39 Å
8HQC Structure of a GPCR-G protein in complex with a natural peptide agonist Deposited 2022-12-13	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 2–351（350 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.89 Å
9KWG Structure of mouse C5a bound mouse C5aR1 in complex with Go Deposited 2024-12-05	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 2–351（350 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.15 Å
9KWX Structure of mouse C5a-desArg bound mouse C5aR1 in complex with Go Deposited 2024-12-06	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 2–351（350 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.13 Å
9KX6 Structure of human C5a-desArg bound mouse C5aR1 in complex with Go Deposited 2024-12-06	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 2–351（350 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.11 Å
9KXS Structure of EP67 bound mouse C5aR1 in complex with Go Deposited 2024-12-07	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 2–351（350 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.31 Å
9KYU Structure of beta-arrestin1 in complex with mouse C5aR1pp Deposited 2024-12-09	Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain U 329–351（23 aa） Chain X 329–351（23 aa）	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	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.72 Å

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

View Construct and Data Evidence

UniProt name	C5AR1_MOUSE
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain U； PDBConstruct 1–23； UniProt 329–351 Author chain V； PDBConstruct 1–23； UniProt 329–351

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	9ky2
Deposition date deposition_date	2024-12-07
最后修订 last_revision	2025-11-26
Structure title title	Structure of beta-arrestin2 in complex with mouse C5aR1pp
Keywords keywords	GPCR, G protein, SIGNALING PROTEIN, beta-arrestin; SIGNALING 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	39.69 Å
Radius of gyration Rg (electron density) rg_electron	39.58 Å
Forward intensity I(0) i0	267006000.00
Molecular weight molecular_weight	132530.0 kDa
Excluded volume excluded_volume	165870 Å³
Envelope volume envelope_volume	224160 Å³
Hydration-shell volume shell_volume	49642 Å³
Envelope diameter envelope_diameter	134.1 Å
Shell Rg shell_rg	42.81 Å
Envelope Rg envelope_rg	39.04 Å
Shape Rg shape_rg	39.58 Å
Total Rg total_rg	39.77 Å
Total atoms total_atoms	9346
Residues n_residues	1187
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	133.2 Å
Rg (real space) rg_real	39.85 Å
Rg uncertainty (real space) rg_real_error	1.58 Å
I(0) (real space) i0_real	2.6700e+08
I(0) uncertainty (real space) i0_real_error	5.0660e+06
Rg (reciprocal space) rg_reciprocal	39.76 Å
I(0) (reciprocal space) i0_reciprocal	267000000.0000
Solution quality estimate total_estimate	0.8820
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	43.3 Å
Skewness Skewness skewness	0.388
Kurtosis Kurtosis kurtosis	-0.451
Angular range angular_range	— – 0.2000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	19750000.0000
Real-space data points n_real_points	41
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.887

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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	Beta-arrestin-2
Molecular weight formula_weight	47217.7 kDa
Mutation mutation	C17G,C60V,L69V,C126S,C141L,C151V,C243V,C252V,C270S,L278F,S280A
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,F
Atom count atom_count	9346

MGEKPGTRVFKKSSPNGKLTVYLGKRDFVDHLDKVDPVDGVVLVDPDYLKDRKVFVTLTVAFRYGREDCDVLGLSFRKDLFIANYQAFPPTPNPPRPPTRLQERLLRKLGQHAHPFFFTIPQNLPSSVTLQPGPEDTGKALGVDFEIRAFVAKSLEEKSHKRNSVRLVIRKVQFAPEKPGPQPSAETTRHFLMSDRSLHLEASLDKELYYHGEPLNVNVHVTNNSTKTVKKIKVSVRQYADIVLFSTAQYKVPVAQVEQDDQVSPSSTFSKVYTITPFLANNREKRGLALDGKLKHEDTNLASSTIVKEGANKEVLGILVSYRVKVKLVVSRGGDVSVELPFVLMHPKPHDHIALPRPQSAATHPPTLLPSAVPETDAPVDTNLIEFETNYATDDDIVFEDFARLRLKGLKDEDYDDQFC

来源 Source

来源生物 organism	Bos taurus
通用名 common_name	domestic cattle
NCBI Class编号 ncbi_taxonomy_id	9913
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Fab30 Heavy Chain
Molecular weight formula_weight	25512.4 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

EISEVQLVESGGGLVQPGGSLRLSCAASGFNVYSSSIHWVRQAPGKGLEWVASISSYYGYTYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSRQFWYSGLDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHHHHHHHH

来源 Source

来源生物 organism	Mus musculus
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Fab30 Light Chain
Molecular weight formula_weight	23435.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,E

SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVPSRFSGSRSGTDFTLTISSLQPEDFATYYCQQYKYVPVTFGQGTKVEIKRTVAAPSVFIFPPSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

来源 Source

来源生物 organism	Mus musculus
NCBI Class编号 ncbi_taxonomy_id	10090
宿主生物 host_organism	Escherichia coli

Entity 4 Entity 4 polymer

Description description	C5a anaphylatoxin chemotactic receptor 1
Molecular weight formula_weight	2892.3 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	V,U

GGGDSKTFTPSTTDTSTRKSQAV

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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	2.78 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	285699

fit	/app/data/saxs_computation/ky/9ky2/9ky2.fit
pddf	/app/data/pr_computation/ky/9ky2/9ky2.pr.out
profile	/app/data/saxs_computation/ky/9ky2/9ky2.dat

Structure of beta-arrestin2 in complex with mouse C5aR1pp

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

Beta-arrestin-2

State in the Current Structure

Other States of the Same Protein in the Database

C5a anaphylatoxin chemotactic receptor 1

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 polymer

Polymer Polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)