7bp2

Structural mechanism directing nucleosome reorganization by NAP1-RELATED PROTEIN 1 (NRP1)

Method: X-RAY DIFFRACTION Dmax: 89.9 Å Quality: GOOD

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

Histone H2A.6

Arabidopsis thaliana

UniProt Q9LD28

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 14–106 Not recorded Histone H2B.1 × 1 (Q9LQQ4) SO4 SULFATE ION × 5 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;291 K;0.2M Sodium sulphate 0.1M Bis Tris propane pH 7.5 20% w/v PEG 3350 Resolution 1.58 Å R-free 0.186
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 14–106 Not recorded Histone H2B.1 × 1 (Q9LQQ4) SO4 SULFATE ION × 5 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;291 K;0.2M Sodium sulphate 0.1M Bis Tris propane pH 7.5 20% w/v PEG 3350 Resolution 1.58 Å R-free 0.186

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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A6_ARATH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–93; UniProt 14–106 Author chain C; PDBConstruct 1–93; UniProt 14–106

Histone H2B.1

Arabidopsis thaliana

UniProt Q9LQQ4

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 51–148 Not recorded Histone H2A.6 × 1 (Q9LD28) SO4 SULFATE ION × 5 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;291 K;0.2M Sodium sulphate 0.1M Bis Tris propane pH 7.5 20% w/v PEG 3350 Resolution 1.58 Å R-free 0.186
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 51–148 Not recorded Histone H2A.6 × 1 (Q9LD28) SO4 SULFATE ION × 5 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;291 K;0.2M Sodium sulphate 0.1M Bis Tris propane pH 7.5 20% w/v PEG 3350 Resolution 1.58 Å R-free 0.186

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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1_ARATH
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–98; UniProt 51–148 Author chain D; PDBConstruct 1–98; UniProt 51–148

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 7bp2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7bp2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7bp2
Deposition date deposition_date2020-03-21
Structure title titleStructural mechanism directing nucleosome reorganization by NAP1-RELATED PROTEIN 1 (NRP1)
Keywords keywordscomplex, Histone, PLANT PROTEIN, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.16
Radius of gyration Rg (electron density) rg_electron24.55
Forward intensity I(0) i027172100.00
Molecular weight molecular_weight39949.0 kDa
Excluded volume excluded_volume50229 ų
Envelope volume envelope_volume60944 ų
Hydration-shell volume shell_volume22170 ų
Envelope diameter envelope_diameter95.6
Shell Rg shell_rg29.73
Envelope Rg envelope_rg24.89
Shape Rg shape_rg24.52
Total Rg total_rg25.30
Total atoms total_atoms2796
Residues n_residues352
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 dmax89.9
Rg (real space) rg_real25.35
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real2.7170e+07
I(0) uncertainty (real space) i0_real_error4.4740e+05
Rg (reciprocal space) rg_reciprocal25.29
I(0) (reciprocal space) i0_reciprocal27170000.0000
Solution quality estimate total_estimate0.8067
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.573
Kurtosis Kurtosis kurtosis-0.175
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7198000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.637; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.638; Smooth: 0.932

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd7bp2a_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd7bp2b_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd7bp2c_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones
Domain ID domain_idd7bp2d_
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.1 — Nucleosome core histones

CATH v4.4 (2 domains)

Domain ID domain_id7bp2B01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id7bp2D01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A

8. Citations (1)

9. Files and Curves (10)