9y9v

THE CRYOEM STRUCTURE OF RHESUS MACAQUE 1A8 AND PGT121 FABS IN COMPLEX WITH BG505 SOSIP.664.

Method: ELECTRON MICROSCOPY Dmax: 192.7 Å Quality: GOOD

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

BG505 SOSIP.664 gp41

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 39 PDB declaration: octadecameric(18) Consistent with protein copy count Chain A; UniProt 30–508 Chain B; UniProt 509–661 Chain C; UniProt 509–661 Chain G; UniProt 30–508 Chain I; UniProt 30–508 Chain J; UniProt 509–661 Not recorded 1A8 Fab heavy chain × 3 1A8 Fab light chain × 3 PGT121 Fab heavy chain × 3 PGT121 Fab light chain × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 27 ;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 ; × 3 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 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 ;alpha-D-mannopyranose-(1-2)-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 ; × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.98 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_9HIV1
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain B; PDBConstruct 1–153; UniProt 509–661 Author chain C; PDBConstruct 1–153; UniProt 509–661 Author chain J; PDBConstruct 1–153; UniProt 509–661 Author chain A; PDBConstruct 1–479; UniProt 30–508 Author chain G; PDBConstruct 1–479; UniProt 30–508 Author chain I; PDBConstruct 1–479; UniProt 30–508

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 9y9v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9y9v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9y9v
Deposition date deposition_date2025-09-15
Structure title titleTHE CRYOEM STRUCTURE OF RHESUS MACAQUE 1A8 AND PGT121 FABS IN COMPLEX WITH BG505 SOSIP.664.
Keywords keywords;HIV-1, ENVELOPE TRIMER, GP120, GP41, VIRAL ENTRY, TYPE-1 MEMBRANE FUSION GLYCOPROTEIN, RHESUS MACAQUE IGG, PGT121, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX, VIRAL PROTEIN, IMMUNE SYSTEM ;; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier58.02
Radius of gyration Rg (electron density) rg_electron57.63
Forward intensity I(0) i02015250000.00
Molecular weight molecular_weight369720.0 kDa
Excluded volume excluded_volume460030 ų
Envelope volume envelope_volume721430 ų
Hydration-shell volume shell_volume105510 ų
Envelope diameter envelope_diameter186.3
Shell Rg shell_rg58.75
Envelope Rg envelope_rg56.27
Shape Rg shape_rg57.66
Total Rg total_rg57.55
Total atoms total_atoms25941
Residues n_residues3009
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 dmax192.7
Rg (real space) rg_real57.75
Rg uncertainty (real space) rg_real_error1.65
I(0) (real space) i0_real2.0150e+09
I(0) uncertainty (real space) i0_real_error3.9050e+07
Rg (reciprocal space) rg_reciprocal58.23
I(0) (reciprocal space) i0_reciprocal2017000000.0000
Solution quality estimate total_estimate0.8651
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary78.5
Skewness Skewness skewness0.100
Kurtosis Kurtosis kurtosis-0.403
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha82460000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.806; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.834

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)