6w16

Crystal structure of a human metapneumovirus monomeric fusion protein complexed with 458 Fab

Method: X-RAY DIFFRACTION Dmax: 136.0 Å Quality: REASONABLE

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

Fusion glycoprotein F0,Envelope glycoprotein fusion

Human immunodeficiency virus 1

UniProt M1E1E4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 1–28 Not recorded 458 Fab heavy chain × 1 458 Fab light chain × 1 ;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 × 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

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.

24 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name M1E1E4_9HIV1
Isoform
PDB entities 1
Chains and sequence ranges Author chain F; PDBConstruct 501–528; UniProt 1–28

Fusion glycoprotein F0,Envelope glycoprotein fusion

Human immunodeficiency virus 1

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 Insufficient information Heteromer Protein × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 1–101 Chain F; UniProt 112–489 Not recorded 458 Fab heavy chain × 1 458 Fab light chain × 1 ;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 × 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

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.

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 F; PDBConstruct 1–101; UniProt 1–101 Author chain F; PDBConstruct 108–485; UniProt 112–489

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 6w16

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6w16
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6w16
Deposition date deposition_date2020-03-03
Structure title titleCrystal structure of a human metapneumovirus monomeric fusion protein complexed with 458 Fab
Keywords keywordsantibody, F protein, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier39.37
Radius of gyration Rg (electron density) rg_electron39.56
Forward intensity I(0) i0127426000.00
Molecular weight molecular_weight89319.0 kDa
Excluded volume excluded_volume111240 ų
Envelope volume envelope_volume164450 ų
Hydration-shell volume shell_volume37783 ų
Envelope diameter envelope_diameter138.5
Shell Rg shell_rg40.98
Envelope Rg envelope_rg39.33
Shape Rg shape_rg39.51
Total Rg total_rg39.80
Total atoms total_atoms6265
Residues n_residues818
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 dmax136.0
Rg (real space) rg_real39.90
Rg uncertainty (real space) rg_real_error0.98
I(0) (real space) i0_real1.2750e+08
I(0) uncertainty (real space) i0_real_error2.0330e+06
Rg (reciprocal space) rg_reciprocal39.56
I(0) (reciprocal space) i0_reciprocal127400000.0000
Solution quality estimate total_estimate0.5947
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.6
Skewness Skewness skewness0.470
Kurtosis Kurtosis kurtosis-0.550
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0334
Highest regularization parameter α highest_alpha12520000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.742; Stabil: 1.000; Sysdev: 0.000; Positv: 1.000; Valcen: 0.586; Smooth: 0.913

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd6w16h_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd6w16l1
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_idd6w16l2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)

CATH v4.4 (4 domains)

Domain ID domain_id6w16H01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6w16H02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6w16L01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6w16L02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)