Current Protein Identity:Q9LQQ4 New Search
Main Difference Dimensions in This Set
Different construct Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
6M2M A role for histone chaperone OsChz1 in histone recognition and deposition Deposited 2020-02-28 Assembly 1 Protein heterocomplex Heteromer;Protein × 15 PDB declaration: pentadecameric(15) Consistent with protein count
Chain B 51–148(98 aa)
Chain D 51–148(98 aa)
Chain F 51–148(98 aa)
Chain H 51–148(98 aa)
Chain J 51–148(98 aa)
Chain L 51–148(98 aa)
Not recorded GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;0.2M Sodium citrate,0.1M Tris-HCl pH 8.5, 30%(w/v)
Resolution 2.85 Å R-free 0.253
7BP2 Structural mechanism directing nucleosome reorganization by NAP1-RELATED PROTEIN 1 (NRP1) Deposited 2020-03-21 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 51–148(98 aa)
Not recorded 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
7BP2 Structural mechanism directing nucleosome reorganization by NAP1-RELATED PROTEIN 1 (NRP1) Deposited 2020-03-21 Assembly 2 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain D 51–148(98 aa)
Not recorded 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
7BP4 Structural insights into nucleosome reorganization by NAP1-RELATED PROTEIN 1 (NRP1) Deposited 2020-03-21 Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count
Chain H 51–148(98 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5.6;290 K;0.7 M ammonium dihydrogen phosphate, 0.07 M sodium citrate and 30% (v/v) glycerol (pH 5.6)
Resolution 2.10 Å R-free 0.226
7BP4 Structural insights into nucleosome reorganization by NAP1-RELATED PROTEIN 1 (NRP1) Deposited 2020-03-21 Assembly 2 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count
Chain B 51–148(98 aa)
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5.6;290 K;0.7 M ammonium dihydrogen phosphate, 0.07 M sodium citrate and 30% (v/v) glycerol (pH 5.6)
Resolution 2.10 Å R-free 0.226
7BP5 Structural insights into nucleosome reorganization by NAP1-RELATED PROTEIN 1 (NRP1) Deposited 2020-03-21 Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count
Chain B 51–148(98 aa)
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;290 K;0.2 M sodium acetate, 20% PEG 3350
Resolution 1.90 Å R-free 0.216
7BP6 Structural insights into nucleosome reorganization by NAP1-RELATED PROTEIN 1 (NRP1) Deposited 2020-03-21 Assembly 1 Protein heterocomplex Heteromer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count
Chain D 51–148(98 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 8.5;290 K;0.2 M sodium nitrate, 0.1 M Bis-Tris propane and 20% (w/v) PEG 3350 (pH 8.5)
Resolution 1.58 Å R-free 0.200
7C7X Structural insights into nucleosome reorganization by NAP1-RELATED PROTEIN 1 (NRP1) Deposited 2020-05-27 Assembly 1 Protein heterocomplex Heteromer;Protein × 6 PDB declaration: hexameric(6) Consistent with protein count
Chain B 51–148(98 aa)
Chain D 51–148(98 aa)
Not recorded GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;291 K;1 M NaCl, 0.1 M sodium cacodylate, 30% (v/v) PEG 600, 10% (v/v) glycerol
Resolution 3.00 Å R-free 0.262
9K3Z Cryo-EM structure of Arabidopsis thaliana H2A.Z-nucleosome with Arabidopsis native 147bp DNA 15.2.2 (C2 symmetry) Deposited 2024-10-21 Assembly 1 Protein–DNA Heteromer;Protein × 8 PDB declaration: decameric(10) Consistent with all polymers
Chain D 1–148(148 aa)
Chain H 1–148(148 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.75 Å
9K40 Cryo-EM structure of Arabidopsis thaliana H2A-nucleosome with Arabidopsis native 147bp DNA 15.2.2 (C2 symmetry) Deposited 2024-10-21 Assembly 1 Protein–DNA Heteromer;Protein × 8 PDB declaration: decameric(10) Consistent with all polymers
Chain D 1–148(148 aa)
Chain H 1–148(148 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.15 Å
9K41 Cryo-EM structure of Arabidopsis thaliana H2A.W-nucleosome with Arabidopsis native 147bp DNA 15.2.2 (C2 symmetry) Deposited 2024-10-21 Assembly 1 Protein–DNA Heteromer;Protein × 8 PDB declaration: decameric(10) Consistent with all polymers
Chain D 1–148(148 aa)
Chain H 1–148(148 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.81 Å
9K42 Cryo-EM structure of Arabidopsis thaliana H2A-nucleosome with 147bp Widom 601 DNA (C2 symmetry) Deposited 2024-10-21 Assembly 1 Protein–DNA Heteromer;Protein × 8 PDB declaration: decameric(10) Consistent with all polymers
Chain D 1–148(148 aa)
Chain H 1–148(148 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.14 Å
9K43 Cryo-EM structure of Arabidopsis thaliana H2A.Z-nucleosome with 147bp Widom 601 DNA (C2 symmetry) Deposited 2024-10-21 Assembly 1 Protein–DNA Heteromer;Protein × 8 PDB declaration: decameric(10) Consistent with all polymers
Chain D 1–148(148 aa)
Chain H 1–148(148 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.87 Å
9K44 Cryo-EM structure of Arabidopsis thaliana H2A-H3.3-nucleosome with Arabidopsis native 147bp DNA 15.2.2 (C2 symmetry) Deposited 2024-10-21 Assembly 1 Protein–DNA Heteromer;Protein × 8 PDB declaration: decameric(10) Consistent with all polymers
Chain D 1–148(148 aa)
Chain H 1–148(148 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.22 Å
9K45 Cryo-EM structure of Arabidopsis thaliana H2A.Z-H3.3-nucleosome with Arabidopsis native 147bp DNA 15.2.2 (C2 symmetry) Deposited 2024-10-21 Assembly 1 Protein–DNA Heteromer;Protein × 8 PDB declaration: decameric(10) Consistent with all polymers
Chain D 1–148(148 aa)
Chain H 1–148(148 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.71 Å
9K46 Cryo-EM structure of Arabidopsis thaliana H2A.W-H3.3-nucleosome with Arabidopsis native 147bp DNA 15.2.2 (C2 symmetry) Deposited 2024-10-21 Assembly 1 Protein–DNA Heteromer;Protein × 8 PDB declaration: decameric(10) Consistent with all polymers
Chain D 1–148(148 aa)
Chain H 1–148(148 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.85 Å