1dsj

NMR SOLUTION STRUCTURE OF VPR50_75, 20 STRUCTURES

Method: SOLUTION NMR Dmax: 47.9 Å Quality: REASONABLE

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

VPR PROTEIN

Human immunodeficiency virus 1

UniProt P12520

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 50–75 Fragment:RESIDUES 50 - 75 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 3.3;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.

8 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPR_HV1N5
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–27; UniProt 50–75

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 1dsj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1dsj
Deposition date deposition_date1997-10-23
Structure title titleNMR SOLUTION STRUCTURE OF VPR50_75, 20 STRUCTURES
Keywords keywordsVIRAL PEPTIDE, POLYPEPTIDE; VIRAL PEPTIDE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.87
Radius of gyration Rg (electron density) rg_electron12.17
Forward intensity I(0) i042958700.00
Molecular weight molecular_weight61453.0 kDa
Excluded volume excluded_volume79589 ų
Envelope volume envelope_volume9475 ų
Hydration-shell volume shell_volume6564 ų
Envelope diameter envelope_diameter51.0
Shell Rg shell_rg18.10
Envelope Rg envelope_rg15.61
Shape Rg shape_rg12.21
Total Rg total_rg12.26
Total atoms total_atoms8860
Residues n_residues520
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 dmax47.9
Rg (real space) rg_real12.28
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real4.2960e+07
I(0) uncertainty (real space) i0_real_error5.3960e+05
Rg (reciprocal space) rg_reciprocal12.26
I(0) (reciprocal space) i0_reciprocal42960000.0000
Solution quality estimate total_estimate0.5401
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary5.5
Skewness Skewness skewness0.618
Kurtosis Kurtosis kurtosis-0.512
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2782.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.007; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.001; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1dsja_
Class classj — Peptides
Fold Fold foldj.11 — VPR protein fragments
Superfamily Superfamily superfamilyj.11.1 — VPR protein fragments
Family Family familyj.11.1.1 — VPR protein fragments

8. Citations (3)

9. Files and Curves (10)