7v1l

Structure of sNASP core in complex with H3 alpha3 helix peptide

Method: X-RAY DIFFRACTION Dmax: 108.6 Å Quality: REASONABLE

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

Isoform 2 of Nuclear autoantigenic sperm protein

Homo sapiens

UniProt P49321-2

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 30–100 Chain B; UniProt 160–340 Not recorded H3 alpha3 helix peptide × 2 (P84243) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1.4M Na-K phosphate, pH 8.2 Resolution 2.85 Å R-free 0.246

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.

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NASP-2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–71; UniProt 30–100 Author chain B; PDBConstruct 72–252; UniProt 160–340

H3 alpha3 helix peptide

Homo sapiens

UniProt P84243

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain V; UniProt 117–136 Not recorded Isoform 2 of Nuclear autoantigenic sperm protein × 2 (P49321-2) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1.4M Na-K phosphate, pH 8.2 Resolution 2.85 Å R-free 0.246

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.

94 other PDB entries and 123 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H33_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain V; PDBConstruct 1–20; UniProt 117–136

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 7v1l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7v1l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7v1l
Deposition date deposition_date2021-08-04
Structure title titleStructure of sNASP core in complex with H3 alpha3 helix peptide
Keywords keywordshistone chaperone, CHAPERONE; CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.10
Radius of gyration Rg (electron density) rg_electron28.82
Forward intensity I(0) i011922300.00
Molecular weight molecular_weight26283.0 kDa
Excluded volume excluded_volume32887 ų
Envelope volume envelope_volume50157 ų
Hydration-shell volume shell_volume16887 ų
Envelope diameter envelope_diameter108.1
Shell Rg shell_rg30.07
Envelope Rg envelope_rg31.55
Shape Rg shape_rg28.80
Total Rg total_rg29.02
Total atoms total_atoms1852
Residues n_residues235
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 dmax108.6
Rg (real space) rg_real29.33
Rg uncertainty (real space) rg_real_error1.74
I(0) (real space) i0_real1.1920e+07
I(0) uncertainty (real space) i0_real_error2.1390e+05
Rg (reciprocal space) rg_reciprocal28.95
I(0) (reciprocal space) i0_reciprocal11920000.0000
Solution quality estimate total_estimate0.6274
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.3
Skewness Skewness skewness0.903
Kurtosis Kurtosis kurtosis-0.083
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha961100.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.106; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.013; Smooth: 0.823

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)