7lbe

CryoEM structure of the HCMV Trimer gHgLgO in complex with neutralizing fabs 13H11 and MSL-109

Method: ELECTRON MICROSCOPY Dmax: 175.2 Å Quality: GOOD

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 × 7 其他Polymer 3 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–715 Not recorded 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 ;alpha-D-mannopyranose-(1-2)-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 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 MAN alpha-D-mannopyranose × 1 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 2.90 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 × 7 其他Polymer 3 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 1–278 Not recorded Envelope glycoprotein H × 1 (Q6SW67) 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 ;alpha-D-mannopyranose-(1-2)-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 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 MAN alpha-D-mannopyranose × 1 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 2.90 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 × 7 其他Polymer 3 PDB declaration: heptameric(7) Consistent with protein copy count Chain C; UniProt 1–464 Not recorded Envelope glycoprotein H × 1 (Q6SW67) Envelope glycoprotein L × 1 (F5HCH8) Fab 13H11 light chain × 1 Fab 13H11 heavy chain × 1 Fab MSL-109 light chain × 1 Fab MSL-109 heavy chain × 1 ;alpha-D-mannopyranose-(1-2)-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 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 MAN alpha-D-mannopyranose × 1 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 2.90 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

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 7lbe

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7lbe
Deposition date deposition_date2021-01-07
Structure title titleCryoEM structure of the HCMV Trimer gHgLgO in complex with 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_guinier53.45
Radius of gyration Rg (electron density) rg_electron54.03
Forward intensity I(0) i0521710000.00
Molecular weight molecular_weight191880.0 kDa
Excluded volume excluded_volume240990 ų
Envelope volume envelope_volume336110 ų
Hydration-shell volume shell_volume56480 ų
Envelope diameter envelope_diameter186.9
Shell Rg shell_rg49.45
Envelope Rg envelope_rg54.19
Shape Rg shape_rg53.98
Total Rg total_rg54.03
Total atoms total_atoms13511
Residues n_residues1653
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 dmax175.2
Rg (real space) rg_real54.06
Rg uncertainty (real space) rg_real_error2.12
I(0) (real space) i0_real5.2170e+08
I(0) uncertainty (real space) i0_real_error1.0670e+07
Rg (reciprocal space) rg_reciprocal52.92
I(0) (reciprocal space) i0_reciprocal520900000.0000
Solution quality estimate total_estimate0.7632
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.3
Skewness Skewness skewness0.555
Kurtosis Kurtosis kurtosis-0.488
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25810000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.733; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.712; Smooth: 0.011

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_idd7lbee_
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_idd7lbeg_
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)