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9os5

Human antibody Fab MPV498 bound to hMPV B2 post-fusion F

Method: ELECTRON MICROSCOPY Dmax: 159.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Fusion glycoprotein F0

human metapneumovirus

UniProt Q6W8S4

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 × 12 PDB declaration: dodecameric（12） Consistent with protein copy count Chain A； UniProt 19–483 Chain B； UniProt 19–483 Chain C； UniProt 19–483 Chain D； UniProt 19–483 Chain E； UniProt 19–483 Chain F； UniProt 19–483 Not recorded MPV498 Fab heavy chain × 3 MPV498 Fab light chain × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 9 ELECTRON MICROSCOPY cryo-EM buffer：pH 7 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.61 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.

Other PDB Difference from Current Entry 9OS5 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
6W16 Crystal structure of a human metapneumovirus monomeric fusion protein complexed with 458 Fab Deposited 2020-03-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric
Chain F 1–101（101 aa）
Chain F 112–489（378 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；0.5 M Ammonium sulfate, 0.1 M Sodium citrate tribasic dihydrate pH 5.6, 1.0 M Lithium sulfate monohydrate
Resolution 3.10 Å R-free 0.234

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q6W8S4_9MONO
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–465； UniProt 19–483 Author chain B； PDBConstruct 1–465； UniProt 19–483 Author chain C； PDBConstruct 1–465； UniProt 19–483 Author chain D； PDBConstruct 1–465； UniProt 19–483 Author chain E； PDBConstruct 1–465； UniProt 19–483 Author chain F； PDBConstruct 1–465； UniProt 19–483

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 9os5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9os5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9os5
Deposition date deposition_date2025-05-23
Structure title titleHuman antibody Fab MPV498 bound to hMPV B2 post-fusion F
Keywords keywordshMPV, Human respiratory disease, cryoem, human metapneumovirus, IMMUNE SYSTEM, ANTIVIRAL PROTEIN; IMMUNE SYSTEM, ANTIVIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier45.95 Å
Radius of gyration Rg (electron density) rg_electron45.95 Å
Forward intensity I(0) i0678665000.00
Molecular weight molecular_weight212150.0 kDa
Excluded volume excluded_volume264710 ų
Envelope volume envelope_volume363040 ų
Hydration-shell volume shell_volume69050 ų
Envelope diameter envelope_diameter172.5 Å
Shell Rg shell_rg47.65 Å
Envelope Rg envelope_rg46.36 Å
Shape Rg shape_rg45.94 Å
Total Rg total_rg46.07 Å
Total atoms total_atoms14885
Residues n_residues1936
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax159.2 Å
Rg (real space) rg_real46.16 Å
Rg uncertainty (real space) rg_real_error1.64 Å
I(0) (real space) i0_real6.7870e+08
I(0) uncertainty (real space) i0_real_error1.3840e+07
Rg (reciprocal space) rg_reciprocal45.95 Å
I(0) (reciprocal space) i0_reciprocal678500000.0000
Solution quality estimate total_estimate0.8559
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary51.5 Å
Skewness Skewness skewness0.498
Kurtosis Kurtosis kurtosis-0.054
Angular range angular_range— – 0.1700 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha57510000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.804; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.712
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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8. Citations (1)

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9. Files and Curves (10)