8aqw

BA.4/5 SARS-CoV-2 Spike bound to mouse ACE2 (local)

Method: ELECTRON MICROSCOPY Dmax: 108.8 Å Quality: GOOD

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

Spike glycoprotein,Fibritin

Enterobacteria phage T4

UniProt P0DTC2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–1208 Not recorded Processed angiotensin-converting enzyme 2,Ig gamma-2A chain C region, A allele × 1 (Q8R0I0,P01863) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

2152 other PDB entries and 2473 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPIKE_SARS2
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–1203; UniProt 1–1208

Spike glycoprotein,Fibritin

Enterobacteria phage T4

UniProt P10104

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 459–484 Not recorded Processed angiotensin-converting enzyme 2,Ig gamma-2A chain C region, A allele × 1 (Q8R0I0,P01863) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

104 other PDB entries and 107 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name WAC_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1208–1232; UniProt 459–484

Processed angiotensin-converting enzyme 2,Ig gamma-2A chain C region, A allele

Mus musculus

UniProt P01863

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 98–330 Not recorded Spike glycoprotein,Fibritin × 1 (P0DTC2,P10104) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

10 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCAA_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 642–874; UniProt 98–330

Processed angiotensin-converting enzyme 2,Ig gamma-2A chain C region, A allele

Mus musculus

UniProt Q8R0I0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 19–615 Not recorded Spike glycoprotein,Fibritin × 1 (P0DTC2,P10104) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

20 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACE2_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 35–631; UniProt 19–615

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 8aqw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8aqw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8aqw
Deposition date deposition_date2022-08-13
Structure title titleBA.4/5 SARS-CoV-2 Spike bound to mouse ACE2 (local)
Keywords keywordsSARS-COV2, omicron, Spike, RBD, mouse, ACE2, ANTIVIRAL PROTEIN, BA4/5, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.57
Radius of gyration Rg (electron density) rg_electron31.14
Forward intensity I(0) i0133364000.00
Molecular weight molecular_weight91314.0 kDa
Excluded volume excluded_volume113890 ų
Envelope volume envelope_volume151410 ų
Hydration-shell volume shell_volume41475 ų
Envelope diameter envelope_diameter117.0
Shell Rg shell_rg37.53
Envelope Rg envelope_rg31.06
Shape Rg shape_rg31.10
Total Rg total_rg31.81
Total atoms total_atoms6442
Residues n_residues789
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 dmax108.8
Rg (real space) rg_real31.65
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real1.3340e+08
I(0) uncertainty (real space) i0_real_error2.2470e+06
Rg (reciprocal space) rg_reciprocal31.62
I(0) (reciprocal space) i0_reciprocal133400000.0000
Solution quality estimate total_estimate0.8565
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.0
Skewness Skewness skewness0.496
Kurtosis Kurtosis kurtosis-0.044
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35600000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.742; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.913

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (2)

9. Files and Curves (10)