7v6o

MERS S ectodomain trimer in complex with neutralizing antibody 111 (state 2)

Method: ELECTRON MICROSCOPY Dmax: 255.3 Å Quality: EXCELLENT

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

Spike glycoprotein

Human betacoronavirus 2c EMC/2012

UniProt K0BRG7

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 18–1206 Chain B; UniProt 18–1206 Chain C; UniProt 18–1206 Not recorded 111 L × 3 111 H × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.56 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.

22 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name K0BRG7_MERS
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1189; UniProt 18–1206 Author chain B; PDBConstruct 1–1189; UniProt 18–1206 Author chain C; PDBConstruct 1–1189; UniProt 18–1206

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 7v6o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7v6o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7v6o
Deposition date deposition_date2021-08-20
Structure title titleMERS S ectodomain trimer in complex with neutralizing antibody 111 (state 2)
Keywords keywordsMERS, spike, antibody, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier70.71
Radius of gyration Rg (electron density) rg_electron70.66
Forward intensity I(0) i03603830000.00
Molecular weight molecular_weight494610.0 kDa
Excluded volume excluded_volume613690 ų
Envelope volume envelope_volume1006600 ų
Hydration-shell volume shell_volume127500 ų
Envelope diameter envelope_diameter222.2
Shell Rg shell_rg62.98
Envelope Rg envelope_rg69.82
Shape Rg shape_rg70.63
Total Rg total_rg70.60
Total atoms total_atoms34804
Residues n_residues4739
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 dmax255.3
Rg (real space) rg_real74.41
Rg uncertainty (real space) rg_real_error1.63
I(0) (real space) i0_real3.6300e+09
I(0) uncertainty (real space) i0_real_error7.3180e+07
Rg (reciprocal space) rg_reciprocal70.51
I(0) (reciprocal space) i0_reciprocal3602000000.0000
Solution quality estimate total_estimate0.9037
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary69.6
Skewness Skewness skewness0.455
Kurtosis Kurtosis kurtosis-0.210
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.9345
Highest regularization parameter α highest_alpha205600000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 0.872; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.788

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)