9dim

Q23.MD39 in Complex with Fab from antibody 35O22

Method: ELECTRON MICROSCOPY Dmax: 152.3 Å Quality: GOOD

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

Q23.MD39 Surface protein gp120

Human immunodeficiency virus 1

UniProt O55774

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 × 10 其他Polymer 29 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 31–497 Chain B; UniProt 502–654 Chain C; UniProt 31–497 Chain D; UniProt 502–654 Chain G; UniProt 31–497 Chain I; UniProt 502–654 Not recorded 35O22 Fab Heavy Chain × 2 35O22 Fab Light Chain × 2 ;alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]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 × 12 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 10 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 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 ; × 3 ;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 19 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6;1X PBS cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.19 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O55774_9HIV1
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–467; UniProt 31–497 Author chain C; PDBConstruct 1–467; UniProt 31–497 Author chain G; PDBConstruct 1–467; UniProt 31–497 Author chain B; PDBConstruct 1–153; UniProt 502–654 Author chain D; PDBConstruct 1–153; UniProt 502–654 Author chain I; PDBConstruct 1–153; UniProt 502–654

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 9dim

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9dim
Deposition date deposition_date2024-09-05
Structure title titleQ23.MD39 in Complex with Fab from antibody 35O22
Keywords keywordsAntibody, Complex, 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_guinier47.65
Radius of gyration Rg (electron density) rg_electron47.05
Forward intensity I(0) i01025040000.00
Molecular weight molecular_weight262360.0 kDa
Excluded volume excluded_volume327000 ų
Envelope volume envelope_volume464340 ų
Hydration-shell volume shell_volume80970 ų
Envelope diameter envelope_diameter152.2
Shell Rg shell_rg52.31
Envelope Rg envelope_rg46.33
Shape Rg shape_rg47.04
Total Rg total_rg47.30
Total atoms total_atoms18385
Residues n_residues2145
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 dmax152.3
Rg (real space) rg_real47.40
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real1.0250e+09
I(0) uncertainty (real space) i0_real_error1.7470e+07
Rg (reciprocal space) rg_reciprocal47.65
I(0) (reciprocal space) i0_reciprocal1025000000.0000
Solution quality estimate total_estimate0.8883
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.6
Skewness Skewness skewness0.119
Kurtosis Kurtosis kurtosis-0.494
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha87560000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.858

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (2)

9. Files and Curves (10)