7mfg

Cryo-EM structure of the VRC310 clinical trial, vaccine-elicited, human antibody 310-030-1D06 Fab in complex with an H1 NC99 HA trimer

Method: ELECTRON MICROSCOPY Dmax: 141.9 Å Quality: GOOD

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

Hemagglutinin HA1 chain

Influenza A virus

UniProt Q6WG00

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 × 12 其他Polymer 3 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 18–343 Chain C; UniProt 18–343 Chain G; UniProt 18–343 Not recorded Hemagglutinin HA2 chain × 3 (Q289M7) 310-030-1D06 Heavy × 3 310-030-1D06 Light × 3 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.87 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6WG00_9INFA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–326; UniProt 18–343 Author chain C; PDBConstruct 1–326; UniProt 18–343 Author chain G; PDBConstruct 1–326; UniProt 18–343

Hemagglutinin HA2 chain

Influenza A virus

UniProt Q289M7

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 × 12 其他Polymer 3 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 344–519 Chain D; UniProt 344–519 Chain I; UniProt 344–519 Not recorded Hemagglutinin HA1 chain × 3 (Q6WG00) 310-030-1D06 Heavy × 3 310-030-1D06 Light × 3 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.87 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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HEMA_I00A1
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–176; UniProt 344–519 Author chain D; PDBConstruct 1–176; UniProt 344–519 Author chain I; PDBConstruct 1–176; UniProt 344–519

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 7mfg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7mfg
Deposition date deposition_date2021-04-09
Structure title titleCryo-EM structure of the VRC310 clinical trial, vaccine-elicited, human antibody 310-030-1D06 Fab in complex with an H1 NC99 HA trimer
Keywords keywordsVRC, IMMUNE SYSTEM, VRC310, H1, Fab, Flu, IMMUNE SYSTEM-Viral protein complex, 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_guinier46.74
Radius of gyration Rg (electron density) rg_electron46.27
Forward intensity I(0) i0896684000.00
Molecular weight molecular_weight241780.0 kDa
Excluded volume excluded_volume299610 ų
Envelope volume envelope_volume428670 ų
Hydration-shell volume shell_volume76379 ų
Envelope diameter envelope_diameter143.4
Shell Rg shell_rg51.09
Envelope Rg envelope_rg45.60
Shape Rg shape_rg46.28
Total Rg total_rg46.43
Total atoms total_atoms17013
Residues n_residues2076
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 dmax141.9
Rg (real space) rg_real46.54
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real8.9670e+08
I(0) uncertainty (real space) i0_real_error1.6620e+07
Rg (reciprocal space) rg_reciprocal46.74
I(0) (reciprocal space) i0_reciprocal896900000.0000
Solution quality estimate total_estimate0.8418
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.3
Skewness Skewness skewness0.128
Kurtosis Kurtosis kurtosis-0.669
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha87280000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.981; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 9 domains

CATH v4.4 (9 domains)

Domain ID domain_id7mfgB01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology20 — Hemagglutinin Ectodomain; Chain B
Homologous superfamily homologous superfamily10
Domain ID domain_id7mfgD01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology20 — Hemagglutinin Ectodomain; Chain B
Homologous superfamily homologous superfamily10
Domain ID domain_id7mfgE01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7mfgF01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7mfgH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7mfgI01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology20 — Hemagglutinin Ectodomain; Chain B
Homologous superfamily homologous superfamily10
Domain ID domain_id7mfgJ01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7mfgK01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7mfgL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)