9mii

253-7A03 Fab in complex with HIV-1 BG505 SOSIP Env trimer and RM20A3 Fab

Method: ELECTRON MICROSCOPY Dmax: 148.6 Å Quality: GOOD

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

HIV-1 Envelope Glycoprotein BG505 SOSIP.664 gp120

Human immunodeficiency virus 1

UniProt Q2N0S6

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 × 14 其他Polymer 8 PDB declaration: 14-meric(14) Consistent with protein copy count Chain A; UniProt 30–505 Chain B; UniProt 509–661 Chain C; UniProt 30–505 Chain D; UniProt 509–661 Chain E; UniProt 30–505 Chain F; UniProt 509–661 Not recorded RM20A3 heavy chain Fv × 3 RM20A3 light chain Fv × 3 253-7A03 heavy chain Fv × 1 253-7A03 lambda chain Fv × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 5 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)-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 ; × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 44 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

186 other PDB entries and 199 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q2N0S6_9HIV1
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 36–511; UniProt 30–505 Author chain C; PDBConstruct 36–511; UniProt 30–505 Author chain E; PDBConstruct 36–511; UniProt 30–505 Author chain B; PDBConstruct 1–153; UniProt 509–661 Author chain D; PDBConstruct 1–153; UniProt 509–661 Author chain F; PDBConstruct 1–153; UniProt 509–661

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 9mii

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9mii
Deposition date deposition_date2024-12-12
Structure title title253-7A03 Fab in complex with HIV-1 BG505 SOSIP Env trimer and RM20A3 Fab
Keywords keywordsHIV-1, SOSIP, germline targeting, VRC01, clinical trial, human, precursor antibody, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.62
Radius of gyration Rg (electron density) rg_electron49.00
Forward intensity I(0) i01341830000.00
Molecular weight molecular_weight298890.0 kDa
Excluded volume excluded_volume371530 ų
Envelope volume envelope_volume527730 ų
Hydration-shell volume shell_volume88358 ų
Envelope diameter envelope_diameter162.0
Shell Rg shell_rg53.82
Envelope Rg envelope_rg48.10
Shape Rg shape_rg48.99
Total Rg total_rg49.20
Total atoms total_atoms20957
Residues n_residues2579
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 dmax148.6
Rg (real space) rg_real49.42
Rg uncertainty (real space) rg_real_error0.96
I(0) (real space) i0_real1.3420e+09
I(0) uncertainty (real space) i0_real_error2.4470e+07
Rg (reciprocal space) rg_reciprocal49.62
I(0) (reciprocal space) i0_reciprocal1342000000.0000
Solution quality estimate total_estimate0.8540
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary60.4
Skewness Skewness skewness0.189
Kurtosis Kurtosis kurtosis-0.542
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha74650000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.974; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.188

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (1)

9. Files and Curves (10)