1a1t

STRUCTURE OF THE HIV-1 NUCLEOCAPSID PROTEIN BOUND TO THE SL3 PSI-RNA RECOGNITION ELEMENT, NMR, 25 STRUCTURES

Method: SOLUTION NMR Dmax: 66.0 Å Quality: REASONABLE

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

NUCLEOCAPSID PROTEIN

Human immunodeficiency virus 1

UniProt Q75677

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–RNA Monomer Protein × 1 RNA 1 PDB declaration: dimeric(2) Consistent with all polymer counts Chain A; UniProt 378–432 Not recorded SL3 STEM-LOOP RNA × 1 ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 6.5;298 K 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q75677_9HIV1
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–55; UniProt 378–432

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 1a1t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1a1t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1a1t
Deposition date deposition_date1997-12-15
Structure title titleSTRUCTURE OF THE HIV-1 NUCLEOCAPSID PROTEIN BOUND TO THE SL3 PSI-RNA RECOGNITION ELEMENT, NMR, 25 STRUCTURES
Keywords keywordsNUCLEOCAPSID PROTEIN, COMPLEX (NUCLEOCAPSID PROTEIN-RNA), STEM-LOOP RNA, Viral protein-RNA COMPLEX; Viral protein/RNA
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.97
Radius of gyration Rg (electron density) rg_electron16.28
Forward intensity I(0) i03160500000.00
Molecular weight molecular_weight325930.0 kDa
Excluded volume excluded_volume345330 ų
Envelope volume envelope_volume30549 ų
Hydration-shell volume shell_volume14537 ų
Envelope diameter envelope_diameter70.4
Shell Rg shell_rg24.24
Envelope Rg envelope_rg19.82
Shape Rg shape_rg16.21
Total Rg total_rg16.51
Total atoms total_atoms37900
Residues n_residues1875
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 dmax66.0
Rg (real space) rg_real16.22
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real3.1610e+09
I(0) uncertainty (real space) i0_real_error4.5060e+07
Rg (reciprocal space) rg_reciprocal16.19
I(0) (reciprocal space) i0_reciprocal3160000000.0000
Solution quality estimate total_estimate0.6913
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.0
Skewness Skewness skewness0.702
Kurtosis Kurtosis kurtosis0.138
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha467100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.294; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.102; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1a1ta_
Class classg — Small proteins
Fold Fold foldg.40 — Retrovirus zinc finger-like domains
Superfamily Superfamily superfamilyg.40.1 — Retrovirus zinc finger-like domains
Family Family familyg.40.1.1 — Retrovirus zinc finger-like domains

CATH v4.4 (1 domains)

Domain ID domain_id1a1tA00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology60 — HIV-1 Nucleocapsid Protein
Homologous superfamily homologous superfamily10 — Zinc finger, CCHC-type

8. Citations (1)

9. Files and Curves (10)