4nft

Crystal structure of human lnkH2B-h2A.Z-Anp32e

Method: X-RAY DIFFRACTION Dmax: 103.5 Å Quality: EXCELLENT

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

Histone H2B type 2-E, Histone H2A.Z

Homo sapiens

UniProt P0C0S5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 16–114 Fragment:UNP residues 34-126, 16-114 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;0.2M Sodium thiocyanate, 20%(w/v) polyethylene glycol 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.61 Å R-free 0.273
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 16–114 Fragment:UNP residues 34-126, 16-114 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;0.2M Sodium thiocyanate, 20%(w/v) polyethylene glycol 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.61 Å R-free 0.273
3 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 16–114 Fragment:UNP residues 34-126, 16-114 Acidic leucine-rich nuclear phosphoprotein 32 family member E × 1 (Q9BTT0) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;0.2M Sodium thiocyanate, 20%(w/v) polyethylene glycol 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.61 Å R-free 0.273
4 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 16–114 Fragment:UNP residues 34-126, 16-114 Acidic leucine-rich nuclear phosphoprotein 32 family member E × 1 (Q9BTT0) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;0.2M Sodium thiocyanate, 20%(w/v) polyethylene glycol 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.61 Å R-free 0.273

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.

25 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2AZ_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 98–196; UniProt 16–114 Author chain B; PDBConstruct 98–196; UniProt 16–114 Author chain C; PDBConstruct 98–196; UniProt 16–114 Author chain D; PDBConstruct 98–196; UniProt 16–114

Histone H2B type 2-E, Histone H2A.Z

Homo sapiens

UniProt Q16778

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 34–126 Fragment:UNP residues 34-126, 16-114 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;0.2M Sodium thiocyanate, 20%(w/v) polyethylene glycol 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.61 Å R-free 0.273
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 34–126 Fragment:UNP residues 34-126, 16-114 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;0.2M Sodium thiocyanate, 20%(w/v) polyethylene glycol 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.61 Å R-free 0.273
3 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 34–126 Fragment:UNP residues 34-126, 16-114 Acidic leucine-rich nuclear phosphoprotein 32 family member E × 1 (Q9BTT0) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;0.2M Sodium thiocyanate, 20%(w/v) polyethylene glycol 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.61 Å R-free 0.273
4 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 34–126 Fragment:UNP residues 34-126, 16-114 Acidic leucine-rich nuclear phosphoprotein 32 family member E × 1 (Q9BTT0) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;0.2M Sodium thiocyanate, 20%(w/v) polyethylene glycol 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.61 Å R-free 0.273

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.

39 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B2E_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–97; UniProt 34–126 Author chain B; PDBConstruct 5–97; UniProt 34–126 Author chain C; PDBConstruct 5–97; UniProt 34–126 Author chain D; PDBConstruct 5–97; UniProt 34–126

Acidic leucine-rich nuclear phosphoprotein 32 family member E

Homo sapiens

UniProt Q9BTT0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
3 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 185–232 Fragment:UNP residues 185-232 Histone H2B type 2-E, Histone H2A.Z × 1 (Q16778,P0C0S5) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;0.2M Sodium thiocyanate, 20%(w/v) polyethylene glycol 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.61 Å R-free 0.273
4 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 185–232 Fragment:UNP residues 185-232 Histone H2B type 2-E, Histone H2A.Z × 1 (Q16778,P0C0S5) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;289 K;0.2M Sodium thiocyanate, 20%(w/v) polyethylene glycol 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K Resolution 2.61 Å R-free 0.273

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AN32E_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 5–52; UniProt 185–232 Author chain F; PDBConstruct 5–52; UniProt 185–232

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 4nft

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4nft
Deposition date deposition_date2013-11-01
Structure title titleCrystal structure of human lnkH2B-h2A.Z-Anp32e
Keywords keywordsHistone binding protein, CHAPERONE; CHAPERONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.82
Radius of gyration Rg (electron density) rg_electron32.03
Forward intensity I(0) i0106188000.00
Molecular weight molecular_weight82035.0 kDa
Excluded volume excluded_volume103160 ų
Envelope volume envelope_volume138630 ų
Hydration-shell volume shell_volume36398 ų
Envelope diameter envelope_diameter109.0
Shell Rg shell_rg38.77
Envelope Rg envelope_rg31.68
Shape Rg shape_rg32.01
Total Rg total_rg32.66
Total atoms total_atoms5772
Residues n_residues746
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 dmax103.5
Rg (real space) rg_real32.71
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real1.0620e+08
I(0) uncertainty (real space) i0_real_error1.6360e+06
Rg (reciprocal space) rg_reciprocal32.76
I(0) (reciprocal space) i0_reciprocal106200000.0000
Solution quality estimate total_estimate0.9055
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary101.4
Skewness Skewness skewness0.146
Kurtosis Kurtosis kurtosis-0.627
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24120000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.947; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.933

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (10 domains)

Domain ID domain_idd4nfta1
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.0 — automated matches
Domain ID domain_idd4nfta2
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.0 — automated matches
Domain ID domain_idd4nfta3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4nftb1
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.0 — automated matches
Domain ID domain_idd4nftb2
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.0 — automated matches
Domain ID domain_idd4nftb3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4nftc1
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.0 — automated matches
Domain ID domain_idd4nftc2
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.0 — automated matches
Domain ID domain_idd4nftd1
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.0 — automated matches
Domain ID domain_idd4nftd2
Class classa — All alpha proteins
Fold Fold folda.22 — Histone-fold
Superfamily Superfamily superfamilya.22.1 — Histone-fold
Family Family familya.22.1.0 — automated matches

CATH v4.4 (4 domains)

Domain ID domain_id4nftA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4nftB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4nftC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology20 — Histone, subunit A
Homologous superfamily homologous superfamily10 — Histone, subunit A
Domain ID domain_id4nftD00
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)