6q05

MERS-CoV S structure in complex with sialyl-lewisX

Method: ELECTRON MICROSCOPY Dmax: 151.1 Å Quality: REASONABLE

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 Other combination Homooligomer Protein × 3 其他Polymer 33 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 19–1294 Chain B; UniProt 19–1294 Chain C; UniProt 19–1294 Not recorded ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 6 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 6 ;N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 FOL FOLIC ACID × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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_9BETC
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 33–1308; UniProt 19–1294 Author chain B; PDBConstruct 33–1308; UniProt 19–1294 Author chain C; PDBConstruct 33–1308; UniProt 19–1294

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 6q05

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6q05
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6q05
Deposition date deposition_date2019-08-01
Structure title titleMERS-CoV S structure in complex with sialyl-lewisX
Keywords keywords;Coronavirus, spike glycoprotein, MERS-CoV, membrane fusion, Structural Genomics, Seattle Structural Genomics Center for Infectious Disease, SSGCID, VIRAL PROTEIN ;; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.53
Radius of gyration Rg (electron density) rg_electron50.13
Forward intensity I(0) i02409380000.00
Molecular weight molecular_weight409530.0 kDa
Excluded volume excluded_volume511420 ų
Envelope volume envelope_volume692550 ų
Hydration-shell volume shell_volume111790 ų
Envelope diameter envelope_diameter159.2
Shell Rg shell_rg56.01
Envelope Rg envelope_rg49.50
Shape Rg shape_rg50.12
Total Rg total_rg50.35
Total atoms total_atoms28782
Residues n_residues3477
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 dmax151.1
Rg (real space) rg_real50.79
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real2.3440e+09
I(0) uncertainty (real space) i0_real_error3.6590e+07
Rg (reciprocal space) rg_reciprocal50.63
I(0) (reciprocal space) i0_reciprocal2410000000.0000
Solution quality estimate total_estimate0.6821
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.5
Skewness Skewness skewness0.230
Kurtosis Kurtosis kurtosis-0.509
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha1.9690
Highest regularization parameter α highest_alpha348700000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.980; Stabil: 0.918; Sysdev: 0.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.203

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)