1acy

CRYSTAL STRUCTURE OF THE PRINCIPAL NEUTRALIZING SITE OF HIV-1

Method: X-RAY DIFFRACTION Dmax: 81.8 Å Quality: EXCELLENT

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

IGG1-KAPPA 59.1 FAB (HEAVY CHAIN)

Mus musculus

UniProt P01869

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain H; UniProt 1–100 Not recorded IGG1-KAPPA 59.1 FAB (LIGHT CHAIN) × 1 HIV-1 GP120 (MN ISOLATE) × 1 (P05877) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 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.

14 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGH1M_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 122–221; UniProt 1–100

HIV-1 GP120 (MN ISOLATE)

HIV-1 M:B_MN

UniProt P05877

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain P; UniProt 306–328 Fragment:FRAGMENT (RESIDUES 308 - 332) IGG1-KAPPA 59.1 FAB (LIGHT CHAIN) × 1 IGG1-KAPPA 59.1 FAB (HEAVY CHAIN) × 1 (P01869) X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 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.

13 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENV_HV1MN
Isoform
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 1–23; UniProt 306–328

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 1acy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1acy
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1acy
Deposition date deposition_date1994-02-10
Structure title titleCRYSTAL STRUCTURE OF THE PRINCIPAL NEUTRALIZING SITE OF HIV-1
Keywords keywordsCOMPLEX(ANTIBODY-HIV-1 FRAGMENT), COMPLEX(ANTIBODY-HIV-1 FRAGMENT) complex; COMPLEX(ANTIBODY/HIV-1 FRAGMENT)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.58
Radius of gyration Rg (electron density) rg_electron24.68
Forward intensity I(0) i041268000.00
Molecular weight molecular_weight48942.0 kDa
Excluded volume excluded_volume60802 ų
Envelope volume envelope_volume73534 ų
Hydration-shell volume shell_volume25144 ų
Envelope diameter envelope_diameter83.8
Shell Rg shell_rg31.69
Envelope Rg envelope_rg24.40
Shape Rg shape_rg24.67
Total Rg total_rg25.48
Total atoms total_atoms3441
Residues n_residues446
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 dmax81.8
Rg (real space) rg_real25.58
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real4.1270e+07
I(0) uncertainty (real space) i0_real_error6.2920e+05
Rg (reciprocal space) rg_reciprocal25.58
I(0) (reciprocal space) i0_reciprocal41270000.0000
Solution quality estimate total_estimate0.9061
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.7
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.509
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8274000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1acyh1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd1acyh2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)
Domain ID domain_idd1acyl1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)
Domain ID domain_idd1acyl2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.2 — C1 set domains (antibody constant domain-like)

CATH v4.4 (4 domains)

Domain ID domain_id1acyH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1acyH02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1acyL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1acyL02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)