4wnn

SPT16-H2A-H2B FACT HISTONE Complex

Method: X-RAY DIFFRACTION Dmax: 107.4 Å Quality: GOOD

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

Histone H2A.1

Saccharomyces cerevisiae

UniProt P04911

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 1–132 Not recorded Histone H2B.1 × 1 (P02293) PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;Crystals of ~ 60 x 60 mm formed within 10 days in 0.1M SPG (succinic acid:sodium dihydrogen phosphate:glycine ) pH 7, 25 % PEG 1500 (A4 of the PACT suite commercial screen (Qiagen). Resolution 1.80 Å R-free 0.225
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–132 Not recorded Histone H2B.1 × 1 (P02293) PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;Crystals of ~ 60 x 60 mm formed within 10 days in 0.1M SPG (succinic acid:sodium dihydrogen phosphate:glycine ) pH 7, 25 % PEG 1500 (A4 of the PACT suite commercial screen (Qiagen). Resolution 1.80 Å R-free 0.225
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1–132 Not recorded Histone H2B.1 × 1 (P02293) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;Crystals of ~ 60 x 60 mm formed within 10 days in 0.1M SPG (succinic acid:sodium dihydrogen phosphate:glycine ) pH 7, 25 % PEG 1500 (A4 of the PACT suite commercial screen (Qiagen). Resolution 1.80 Å R-free 0.225
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–132 Not recorded Histone H2B.1 × 1 (P02293) SPT16 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;Crystals of ~ 60 x 60 mm formed within 10 days in 0.1M SPG (succinic acid:sodium dihydrogen phosphate:glycine ) pH 7, 25 % PEG 1500 (A4 of the PACT suite commercial screen (Qiagen). Resolution 1.80 Å R-free 0.225

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.

20 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–132; UniProt 1–132 Author chain C; PDBConstruct 1–132; UniProt 1–132 Author chain E; PDBConstruct 1–132; UniProt 1–132 Author chain G; PDBConstruct 1–132; UniProt 1–132

Histone H2B.1

Saccharomyces cerevisiae

UniProt P02293

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 31–131 Fragment:UNP residues 31-131 Histone H2A.1 × 1 (P04911) PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;Crystals of ~ 60 x 60 mm formed within 10 days in 0.1M SPG (succinic acid:sodium dihydrogen phosphate:glycine ) pH 7, 25 % PEG 1500 (A4 of the PACT suite commercial screen (Qiagen). Resolution 1.80 Å R-free 0.225
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 31–131 Fragment:UNP residues 31-131 Histone H2A.1 × 1 (P04911) PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;Crystals of ~ 60 x 60 mm formed within 10 days in 0.1M SPG (succinic acid:sodium dihydrogen phosphate:glycine ) pH 7, 25 % PEG 1500 (A4 of the PACT suite commercial screen (Qiagen). Resolution 1.80 Å R-free 0.225
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 31–131 Fragment:UNP residues 31-131 Histone H2A.1 × 1 (P04911) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;Crystals of ~ 60 x 60 mm formed within 10 days in 0.1M SPG (succinic acid:sodium dihydrogen phosphate:glycine ) pH 7, 25 % PEG 1500 (A4 of the PACT suite commercial screen (Qiagen). Resolution 1.80 Å R-free 0.225
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 31–131 Fragment:UNP residues 31-131 Histone H2A.1 × 1 (P04911) SPT16 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;277 K;Crystals of ~ 60 x 60 mm formed within 10 days in 0.1M SPG (succinic acid:sodium dihydrogen phosphate:glycine ) pH 7, 25 % PEG 1500 (A4 of the PACT suite commercial screen (Qiagen). Resolution 1.80 Å R-free 0.225

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.

23 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–102; UniProt 31–131 Author chain D; PDBConstruct 2–102; UniProt 31–131 Author chain F; PDBConstruct 2–102; UniProt 31–131 Author chain H; PDBConstruct 2–102; UniProt 31–131

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 4wnn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4wnn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4wnn
Deposition date deposition_date2014-10-13
Structure title titleSPT16-H2A-H2B FACT HISTONE Complex
Keywords keywordsFACT, SPT16, Histone, POB3, H2A, H2B, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.60
Radius of gyration Rg (electron density) rg_electron30.69
Forward intensity I(0) i0105349000.00
Molecular weight molecular_weight81553.0 kDa
Excluded volume excluded_volume102660 ų
Envelope volume envelope_volume132810 ų
Hydration-shell volume shell_volume36424 ų
Envelope diameter envelope_diameter114.8
Shell Rg shell_rg37.48
Envelope Rg envelope_rg30.59
Shape Rg shape_rg30.65
Total Rg total_rg31.43
Total atoms total_atoms5739
Residues n_residues731
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 dmax107.4
Rg (real space) rg_real31.55
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real1.0530e+08
I(0) uncertainty (real space) i0_real_error1.7940e+06
Rg (reciprocal space) rg_reciprocal31.57
I(0) (reciprocal space) i0_reciprocal105400000.0000
Solution quality estimate total_estimate0.8685
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.0
Skewness Skewness skewness0.307
Kurtosis Kurtosis kurtosis-0.159
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22470000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.786; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.931

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd4wnna_
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_idd4wnnb_
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_idd4wnnc_
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_idd4wnnd_
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_idd4wnne_
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_idd4wnnf_
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_idd4wnng_
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_idd4wnnh_
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 (8 domains)

Domain ID domain_id4wnnA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4wnnB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4wnnC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4wnnD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4wnnE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4wnnF00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4wnnG00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4wnnH00
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)