2rvq

Solution structure of the isolated histone H2A-H2B heterodimer

Method: SOLUTION NMR Dmax: 81.3 Å Quality: REASONABLE

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

Histone H2A type 1-B/E

Homo sapiens

UniProt P04908

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 C; UniProt 1–130 Not recorded Histone H2B type 1-J × 1 (P06899) SOLUTION NMR NMR measurement conditions:pH 6;293 K;Ionic strength (raw mmCIF value) 400;Pressure ambient NMR sample composition:0.1-0.3 mM [U-13C; U-15N; U-2H] entity_1-1, 0.1-0.3 mM [U-13C; U-15N; U-2H] entity_2-2, 90% H2O/10% D2O | 90% H2O/10% D2O 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.

343 other PDB entries and 350 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 4–133; UniProt 1–130

Histone H2B type 1-J

Homo sapiens

UniProt P06899

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 D; UniProt 1–126 Not recorded Histone H2A type 1-B/E × 1 (P04908) SOLUTION NMR NMR measurement conditions:pH 6;293 K;Ionic strength (raw mmCIF value) 400;Pressure ambient NMR sample composition:0.1-0.3 mM [U-13C; U-15N; U-2H] entity_1-1, 0.1-0.3 mM [U-13C; U-15N; U-2H] entity_2-2, 90% H2O/10% D2O | 90% H2O/10% D2O 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.

290 other PDB entries and 301 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1J_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 4–129; UniProt 1–126

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 2rvq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2rvq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2rvq
Deposition date deposition_date2016-03-28
Structure title titleSolution structure of the isolated histone H2A-H2B heterodimer
Keywords keywordsnucleosome, histone, H2A, H2B, DNA binding protein, CS-Rosetta, NUCLEAR PROTEIN-NUCLEAR PROTEIN complex; NUCLEAR PROTEIN/NUCLEAR PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier29.58
Radius of gyration Rg (electron density) rg_electron29.20
Forward intensity I(0) i01164120000.00
Molecular weight molecular_weight284970.0 kDa
Excluded volume excluded_volume359100 ų
Envelope volume envelope_volume304180 ų
Hydration-shell volume shell_volume61957 ų
Envelope diameter envelope_diameter164.2
Shell Rg shell_rg45.27
Envelope Rg envelope_rg43.05
Shape Rg shape_rg29.11
Total Rg total_rg30.18
Total atoms total_atoms41410
Residues n_residues2620
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 dmax81.3
Rg (real space) rg_real27.44
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real1.1110e+09
I(0) uncertainty (real space) i0_real_error1.5140e+07
Rg (reciprocal space) rg_reciprocal29.94
I(0) (reciprocal space) i0_reciprocal1164000000.0000
Solution quality estimate total_estimate0.6668
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.496
Kurtosis Kurtosis kurtosis-0.459
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha1.6820
Highest regularization parameter α highest_alpha5744000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.931; Stabil: 0.991; Sysdev: 0.000; Positv: 1.000; Valcen: 0.904; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id2rvqC01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id2rvqD00
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)