9pit

HIV-1 bnAb 1-23 in complex with BG505 MD39 SOSIP and RM19R

Method: ELECTRON MICROSCOPY Dmax: 157.9 Å Quality: GOOD

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

Envelope glycoprotein gp160

Human immunodeficiency virus 1

UniProt Q2N0S5

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 × 18 其他Polymer 33 PDB declaration: 18-meric(18) Consistent with protein copy count Chain B; UniProt 30–510 Chain E; UniProt 30–510 Chain F; UniProt 30–510 Mutation:T106E, M271I, F288L, R304V, A319Y, T332N, N363Q, A501C, E509R, K510R, A512R, V513R 1-23 light chain Fv × 3 1-23 heavy chain Fv × 3 RM19R light chain Fv × 3 RM19R heavy chain Fv × 3 Envelope glycoprotein gp41 - BG505 MD39 × 3 (Q2N0S8) ;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 ; × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 24 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

53 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q2N0S5_HV1
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 32–512; UniProt 30–510 Author chain E; PDBConstruct 32–512; UniProt 30–510 Author chain F; PDBConstruct 32–512; UniProt 30–510

Envelope glycoprotein gp41 - BG505 MD39

Human immunodeficiency virus 1

UniProt Q2N0S8

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 × 18 其他Polymer 33 PDB declaration: 18-meric(18) Consistent with protein copy count Chain A; UniProt 511–663 Chain C; UniProt 511–663 Chain D; UniProt 511–663 Mutation:F519S, I559P, A561P, L568D, V570H, R585H, T605C 1-23 light chain Fv × 3 1-23 heavy chain Fv × 3 Envelope glycoprotein gp160 × 3 (Q2N0S5) RM19R light chain Fv × 3 RM19R heavy chain Fv × 3 ;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 ; × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 24 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q2N0S8_9HIV1
Isoform
PDB entities 6
Chains and sequence ranges Author chain A; PDBConstruct 1–153; UniProt 511–663 Author chain C; PDBConstruct 1–153; UniProt 511–663 Author chain D; PDBConstruct 1–153; UniProt 511–663

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 9pit

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9pit
Deposition date deposition_date2025-07-11
Structure title titleHIV-1 bnAb 1-23 in complex with BG505 MD39 SOSIP and RM19R
Keywords keywordsHIV-1, SOSIP, human, broadly neutralizing antibody, Fab, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier50.16
Radius of gyration Rg (electron density) rg_electron49.71
Forward intensity I(0) i01971160000.00
Molecular weight molecular_weight363580.0 kDa
Excluded volume excluded_volume451940 ų
Envelope volume envelope_volume635010 ų
Hydration-shell volume shell_volume102880 ų
Envelope diameter envelope_diameter159.5
Shell Rg shell_rg56.15
Envelope Rg envelope_rg48.75
Shape Rg shape_rg49.69
Total Rg total_rg49.97
Total atoms total_atoms25533
Residues n_residues3000
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 dmax157.9
Rg (real space) rg_real49.96
Rg uncertainty (real space) rg_real_error1.02
I(0) (real space) i0_real1.9710e+09
I(0) uncertainty (real space) i0_real_error3.5410e+07
Rg (reciprocal space) rg_reciprocal50.30
I(0) (reciprocal space) i0_reciprocal1972000000.0000
Solution quality estimate total_estimate0.8956
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.1
Skewness Skewness skewness0.112
Kurtosis Kurtosis kurtosis-0.591
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha163000000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.862

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)