7lbf

CryoEM structure of the HCMV Trimer gHgLgO in complex with human Platelet-derived growth factor receptor alpha and neutralizing fabs 13H11 and MSL-109

Method: ELECTRON MICROSCOPY Dmax: 174.6 Å Quality: REASONABLE

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

Envelope glycoprotein H

Human cytomegalovirus (strain Merlin)

UniProt Q6SW67

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 Heteromer Protein × 8 其他Polymer 3 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–715 Not recorded Envelope glycoprotein L × 1 (F5HCH8) Envelope glycoprotein O × 1 (Q8BCU3) Isoform 3 of Platelet-derived growth factor receptor alpha × 1 (P16234) Fab 13H11 light chain × 1 Fab 13H11 heavy chain × 1 Fab MSL-109 light chain × 1 Fab MSL-109 heavy chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[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 ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;The sample was gently cross-linked with 0.025% (v/v) EM-grade glutaraldehyde for 10 min at RT and quenched with 9 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 2.5 seconds before plunging 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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GH_HCMVM
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–715; UniProt 1–715

Envelope glycoprotein L

Human cytomegalovirus (strain Merlin)

UniProt F5HCH8

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 Heteromer Protein × 8 其他Polymer 3 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–278 Not recorded Envelope glycoprotein H × 1 (Q6SW67) Envelope glycoprotein O × 1 (Q8BCU3) Isoform 3 of Platelet-derived growth factor receptor alpha × 1 (P16234) Fab 13H11 light chain × 1 Fab 13H11 heavy chain × 1 Fab MSL-109 light chain × 1 Fab MSL-109 heavy chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[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 ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;The sample was gently cross-linked with 0.025% (v/v) EM-grade glutaraldehyde for 10 min at RT and quenched with 9 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 2.5 seconds before plunging 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GL_HCMVM
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–278; UniProt 1–278

Envelope glycoprotein O

Human cytomegalovirus

UniProt Q8BCU3

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 Heteromer Protein × 8 其他Polymer 3 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 1–464 Not recorded Envelope glycoprotein H × 1 (Q6SW67) Envelope glycoprotein L × 1 (F5HCH8) Isoform 3 of Platelet-derived growth factor receptor alpha × 1 (P16234) Fab 13H11 light chain × 1 Fab 13H11 heavy chain × 1 Fab MSL-109 light chain × 1 Fab MSL-109 heavy chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[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 ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;The sample was gently cross-linked with 0.025% (v/v) EM-grade glutaraldehyde for 10 min at RT and quenched with 9 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 2.5 seconds before plunging 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8BCU3_HCMV
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–464; UniProt 1–464

Isoform 3 of Platelet-derived growth factor receptor alpha

Homo sapiens

UniProt P16234

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 Heteromer Protein × 8 其他Polymer 3 PDB declaration: octameric(8) Consistent with protein copy count Chain D; UniProt 1–524 Not recorded Envelope glycoprotein H × 1 (Q6SW67) Envelope glycoprotein L × 1 (F5HCH8) Envelope glycoprotein O × 1 (Q8BCU3) Fab 13H11 light chain × 1 Fab 13H11 heavy chain × 1 Fab MSL-109 light chain × 1 Fab MSL-109 heavy chain × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[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 ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;The sample was gently cross-linked with 0.025% (v/v) EM-grade glutaraldehyde for 10 min at RT and quenched with 9 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 2.5 seconds before plunging 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PGFRA_HUMAN
Isoform P16234-3
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–524; UniProt 1–524

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 7lbf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7lbf
Deposition date deposition_date2021-01-07
Structure title titleCryoEM structure of the HCMV Trimer gHgLgO in complex with human Platelet-derived growth factor receptor alpha and neutralizing fabs 13H11 and MSL-109
Keywords keywordsvirus, receptor, complex, neutralizing antibody, VIRAL PROTEIN, VIRAL PROTEIN-Immune System complex; VIRAL PROTEIN/Immune System
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.36
Radius of gyration Rg (electron density) rg_electron56.97
Forward intensity I(0) i0694820000.00
Molecular weight molecular_weight222390.0 kDa
Excluded volume excluded_volume279180 ų
Envelope volume envelope_volume398540 ų
Hydration-shell volume shell_volume62569 ų
Envelope diameter envelope_diameter186.5
Shell Rg shell_rg52.20
Envelope Rg envelope_rg56.30
Shape Rg shape_rg56.93
Total Rg total_rg56.96
Total atoms total_atoms15656
Residues n_residues1923
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 dmax174.6
Rg (real space) rg_real56.92
Rg uncertainty (real space) rg_real_error1.94
I(0) (real space) i0_real6.9480e+08
I(0) uncertainty (real space) i0_real_error1.4760e+07
Rg (reciprocal space) rg_reciprocal55.84
I(0) (reciprocal space) i0_reciprocal693700000.0000
Solution quality estimate total_estimate0.5721
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.6
Skewness Skewness skewness0.456
Kurtosis Kurtosis kurtosis-0.686
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33600000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.850; Stabil: 0.997; Sysdev: 0.041; Positv: 1.000; Valcen: 0.768; Smooth: 0.001

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd7lbfe_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.0 — automated matches
Domain ID domain_idd7lbfg_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.0 — automated matches

8. Citations (1)

9. Files and Curves (10)