7r7p

Immature HIV-1 CACTD-SP1 lattice with Bevirimat (BVM) and Inositol hexakisphosphate (IP6)

Method: SOLID-STATE NMR Dmax: 80.0 Å Quality: EXCELLENT

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

Gag polyprotein

Human immunodeficiency virus 1

UniProt Q72497

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain G; UniProt 278–377 Chain H; UniProt 278–377 Chain I; UniProt 278–377 Chain J; UniProt 278–377 Chain K; UniProt 278–377 Chain L; UniProt 278–377 Mutation:P241T IHP INOSITOL HEXAKISPHOSPHATE × 1 2I4 3alpha-[(3-carboxy-3-methylbutanoyl)oxy]-8alpha,9beta,10alpha,13alpha,17alpha,19beta-lup-20(29)-en-28-oic acid × 1 SOLID-STATE NMR NMR measurement conditions:pH 8;277.15 K;Ionic strength (raw mmCIF value) 250;Pressure 1 NMR measurement conditions:pH 8;263.15 K;Ionic strength (raw mmCIF value) 250;Pressure 1 NMR measurement conditions:pH 8;277.15 K;Ionic strength (raw mmCIF value) 250;Pressure 1 NMR measurement conditions:pH 8;268.15 K;Ionic strength (raw mmCIF value) 250;Pressure 1 NMR sample composition:400 uM [U-100% 13C; U-100% 15N] HIV-1 CACTD-SP1, 400 uM IP6, 360 uM BVM, Protein buffer | Protein buffer NMR sample composition:400 uM [U-100% 13C; U-100% 15N; 99.9%-2H] HIV-1 CACTD-SP1, 400 uM IP6, 360 uM Bevirimat, protein buffer | protein buffer Resolution not provided

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.

27 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q72497_9HIV1
Isoform
PDB entities 1
Chains and sequence ranges Author chain G; PDBConstruct 3–102; UniProt 278–377 Author chain H; PDBConstruct 3–102; UniProt 278–377 Author chain I; PDBConstruct 3–102; UniProt 278–377 Author chain J; PDBConstruct 3–102; UniProt 278–377 Author chain K; PDBConstruct 3–102; UniProt 278–377 Author chain L; PDBConstruct 3–102; UniProt 278–377

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 7r7p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7r7p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7r7p
Deposition date deposition_date2021-06-25
Structure title titleImmature HIV-1 CACTD-SP1 lattice with Bevirimat (BVM) and Inositol hexakisphosphate (IP6)
Keywords keywordsHIV-1 capsid, maturation inhibitors, HIV-AIDS, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLID-STATE NMR

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

Radius of gyration Rg (Guinier) rg_guinier26.14
Radius of gyration Rg (electron density) rg_electron25.98
Forward intensity I(0) i01748290000.00
Molecular weight molecular_weight338710.0 kDa
Excluded volume excluded_volume419240 ų
Envelope volume envelope_volume120170 ų
Hydration-shell volume shell_volume35888 ų
Envelope diameter envelope_diameter88.5
Shell Rg shell_rg35.32
Envelope Rg envelope_rg27.01
Shape Rg shape_rg25.99
Total Rg total_rg26.19
Total atoms total_atoms47220
Residues n_residues3060
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 dmax80.0
Rg (real space) rg_real25.99
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real1.7480e+09
I(0) uncertainty (real space) i0_real_error2.3700e+07
Rg (reciprocal space) rg_reciprocal26.04
I(0) (reciprocal space) i0_reciprocal1748000000.0000
Solution quality estimate total_estimate0.9111
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.8
Skewness Skewness skewness0.115
Kurtosis Kurtosis kurtosis-0.538
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6859000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)