SAXSdb — 1roc

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

Anti-silencing protein 1

Saccharomyces cerevisiae

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 2–154	Not recorded	BR BROMIDE ION × 9	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；PEG 3350, sodium bromide, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.50 Å R-free 0.246

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.

Other PDB	Difference from Current Entry 1ROC	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1WG3 Structural analysis of yeast nucleosome-assembly factor CIA1p Deposited 2004-05-27	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–169（169 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG8K, AS, Tris-HCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 3.00 Å R-free 0.274
2HUE Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4 Deposited 2006-07-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 2–169（168 aa） Fragment：residues 2-169	Not recorded	ZN ZINC ION × 1 GOL GLYCEROL × 2 SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.1M potassium sulfate, 0.1M Tris-HCl, 14.5% PEG 4K, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.70 Å R-free 0.239
2HUE Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4 Deposited 2006-07-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 2–169（168 aa） Fragment：residues 2-169	Not recorded	ZN ZINC ION × 2 GOL GLYCEROL × 4 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.1M potassium sulfate, 0.1M Tris-HCl, 14.5% PEG 4K, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.70 Å R-free 0.239
2HUE Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4 Deposited 2006-07-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 2–169（168 aa） Fragment：residues 2-169	Not recorded	ZN ZINC ION × 2 GOL GLYCEROL × 4 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.1M potassium sulfate, 0.1M Tris-HCl, 14.5% PEG 4K, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.70 Å R-free 0.239
2HUE Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4 Deposited 2006-07-26	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 2–169（168 aa） Fragment：residues 2-169	Not recorded	ZN ZINC ION × 2 GOL GLYCEROL × 4 SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295 K；0.1M potassium sulfate, 0.1M Tris-HCl, 14.5% PEG 4K, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 1.70 Å R-free 0.239
2IDC Structure of the Histone H3-Asf1 Chaperone Interaction Deposited 2006-09-14	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–155（154 aa） Fragment：Asf1, residues 2-155 and H3, residues 121-134	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；292 K；Tris-HCl, Li2SO4, PEG 4000, glycerol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K	Resolution 2.20 Å R-free 0.239
2YGV Conserved N-terminal domain of the yeast Histone Chaperone Asf1 in complex with the C-terminal fragment of Rad53 Deposited 2011-04-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–156（156 aa） Fragment：CONSERVED N-TERMINAL DOMAIN, RESIDUES 1-156	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；5% PEG 8000, 0.1M NACACO PH 6, 0.2M MG ACETATE	Resolution 2.94 Å R-free 0.257
2YGV Conserved N-terminal domain of the yeast Histone Chaperone Asf1 in complex with the C-terminal fragment of Rad53 Deposited 2011-04-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–156（156 aa） Fragment：CONSERVED N-TERMINAL DOMAIN, RESIDUES 1-156	Not recorded	SO4 SULFATE ION × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；5% PEG 8000, 0.1M NACACO PH 6, 0.2M MG ACETATE	Resolution 2.94 Å R-free 0.257
2YGV Conserved N-terminal domain of the yeast Histone Chaperone Asf1 in complex with the C-terminal fragment of Rad53 Deposited 2011-04-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–156（156 aa） Fragment：CONSERVED N-TERMINAL DOMAIN, RESIDUES 1-156	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；5% PEG 8000, 0.1M NACACO PH 6, 0.2M MG ACETATE	Resolution 2.94 Å R-free 0.257
2YGV Conserved N-terminal domain of the yeast Histone Chaperone Asf1 in complex with the C-terminal fragment of Rad53 Deposited 2011-04-21	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–156（156 aa） Fragment：CONSERVED N-TERMINAL DOMAIN, RESIDUES 1-156	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；5% PEG 8000, 0.1M NACACO PH 6, 0.2M MG ACETATE	Resolution 2.94 Å R-free 0.257
4EO5 Yeast Asf1 bound to H3/H4G94P mutant Deposited 2012-04-13	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 2–169（168 aa） Fragment：residues 2-169	Not recorded	ACT ACETATE ION × 2 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.9；298 K；7.14% PEG 3350, 0.2 M Magnesium Acetate, pH 7.9, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.35 Å R-free 0.240
4ZBJ UBN1 peptide bound to H3.3/H4/Asf1 Deposited 2015-04-14	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 2–169（168 aa） Fragment：UNP residues 2-169	Not recorded	CL CHLORIDE ION × 8 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；295 K；0.1 M Sodium Cacodylate pH 6.0, 8% PEG 8K, 0.2 M NaCl	Resolution 2.25 Å R-free 0.235
5EII Structural determination of an protein complex of a Fab with increased solubility Deposited 2015-10-29	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain I 1–156（156 aa） Fragment：UNP residues 1-156	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions LIQUID DIFFUSION；293 K；Crystals were grown by hanging drop liquid diffusion by adding a solution containing 20% PEG 3350 and Sodium Acetate, pH 5.5	Resolution 2.44 Å R-free 0.233
5EII Structural determination of an protein complex of a Fab with increased solubility Deposited 2015-10-29	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 1–156（156 aa） Fragment：UNP residues 1-156	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions LIQUID DIFFUSION；293 K；Crystals were grown by hanging drop liquid diffusion by adding a solution containing 20% PEG 3350 and Sodium Acetate, pH 5.5	Resolution 2.44 Å R-free 0.233
5UCB Structure of antigen-Fab complex with engineered switch residue region. Deposited 2016-12-22	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 2–154（153 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；18% PEG3350,	Resolution 1.52 Å R-free 0.169
5UEA Structure of antigen-Fab complex with Histone chaperone ASF1 Deposited 2016-12-29	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain X 2–154（153 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% PEG 3350, .2 M Ammonium chloride	Resolution 1.70 Å R-free 0.207
5UEA Structure of antigen-Fab complex with Histone chaperone ASF1 Deposited 2016-12-29	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 2–154（153 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% PEG 3350, .2 M Ammonium chloride	Resolution 1.70 Å R-free 0.207
5UEK Structure of antigen-Fab 12E complex with Histone chaperone ASF1 Deposited 2017-01-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 2–154（153 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% PEG 3350, 20% ethylene glycol, .2 M Ammonium Acetate	Resolution 1.70 Å R-free 0.212
6AYZ Crystal structure of Asf1-Fab 12E complex Deposited 2017-09-08	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 2–154（153 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.1；298 K；0.2 M Ammonium Acetate, 20% PEG 3350	Resolution 2.10 Å R-free 0.236
6AYZ Crystal structure of Asf1-Fab 12E complex Deposited 2017-09-08	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain M 2–154（153 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.1；298 K；0.2 M Ammonium Acetate, 20% PEG 3350	Resolution 2.10 Å R-free 0.236
6AZ2 Crystal structure of Asf1-Fab 12E complex Deposited 2017-09-09	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 2–154（153 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.1；298 K；20% PEG3350, 0.2 M ammonium acetate	Resolution 2.48 Å R-free 0.228
6AZ2 Crystal structure of Asf1-Fab 12E complex Deposited 2017-09-09	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain D 2–154（153 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.1；298 K；20% PEG3350, 0.2 M ammonium acetate	Resolution 2.48 Å R-free 0.228
6F0Y Rtt109 peptide bound to Asf1 Deposited 2017-11-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2–169（168 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.2；298 K；Ionic strength (raw mmCIF value) 150；Pressure ambient NMR measurement conditions pH 6.2；298 K；Ionic strength (raw mmCIF value) 150；Pressure ambient NMR sample composition 0.5 mM [U-99% 13C; U-99% 15N] Histone chaperone Asf1, 3 mM histone acetyltransferase Rtt109 C-terminus, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.15 mM [U-99% 13C; U-99% 15N] Histone chaperone Asf1, 0.5 mM histone acetyltransferase Rtt109 C-terminus, 100% D2O \| 100% D2O NMR sample composition 0.5 mM [U-99% 13C; U-99% 15N; U-99% 2D] Histone chaperone ASF1, 0.15 mM histone acetyltransferase Rtt109 C-terminus, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6O22 Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate. Deposited 2019-02-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 2–279（278 aa）	Not recorded	No recorded non-water small molecule	Experimental method not declared NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 150；Pressure 1 NMR sample composition 70 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 70 uM Rtt109, 70 uM Asf1, 70 uM H3, 70 uM H4, 100% D2O \| 100% D2O NMR sample composition 70 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 70 uM Rtt109, 70 uM Asf1, 70 uM H3(110A,63C) mutant with a cysteine coupled to a paramagnetic tag, 70 uM H4, 100% D2O \| 100% D2O NMR sample composition 90 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 90 uM Rtt109, 90 uM Asf1, 90 uM H3(110A,76C) mutant with a cysteine coupled to a paramagnetic tag, 90 uM H4, 100% D2O \| 100% D2O NMR sample composition 30 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 30 uM Rtt109, 30 uM Asf1, 30 uM H3, 30 uM H4(30C) mutant with a cysteine coupled to a paramagnetic tag, 100% D2O \| 100% D2O NMR sample composition 70 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 70 uM Rtt109, 70 uM Asf1, 70 uM H3, 70 uM H4(82C) mutant with a cysteine coupled to a paramagnetic tag, 100% D2O \| 100% D2O NMR sample composition 80 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 80 uM Rtt109, 80 uM Asf1, 80 uM H3, 80 uM H4(45C) mutant with a cysteine coupled to a paramagnetic tag, 100% D2O \| 100% D2O NMR sample composition 30 uM ILV methyl labelled, perdeuterated Vps75 (dimer), 30 uM Rtt109, 30 uM Asf1, 30 uM H3, 30 uM H4(93C) mutant with a cysteine coupled to a paramagnetic tag, 100% D2O \| 100% D2O	Resolution not provided
9AVO The crystal structure of an engineered Protein GD with Human Kappa Fab Deposited 2024-03-04	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 2–159（158 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；293 K；0.1M Sodium cacodylate pH 6.8 and 0.8M Sodium citrate tribasic	Resolution 3.00 Å R-free 0.241
9AWE The crystal structure of an engineered Protein GF with Human Kappa Fab Deposited 2024-03-05	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 2–159（158 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1M Sodium Cacodylate pH 6.0, 0.1M Calcium acetate hydrate, 10% PEG 8000	Resolution 2.80 Å R-free 0.293

16 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ASF1_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–155； UniProt 2–154

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1roc
Deposition date deposition_date	2003-12-02
Structure title title	Crystal structure of the histone deposition protein Asf1
Keywords keywords	beta-sandwich, REPLICATION, CHAPERONE; REPLICATION, CHAPERONE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	18.42 Å
Radius of gyration Rg (electron density) rg_electron	17.41 Å
Forward intensity I(0) i0	6706320.00
Molecular weight molecular_weight	18174.0 kDa
Excluded volume excluded_volume	22286 Å³
Envelope volume envelope_volume	26235 Å³
Hydration-shell volume shell_volume	13638 Å³
Envelope diameter envelope_diameter	64.6 Å
Shell Rg shell_rg	22.16 Å
Envelope Rg envelope_rg	17.73 Å
Shape Rg shape_rg	17.34 Å
Total Rg total_rg	18.42 Å
Total atoms total_atoms	1244
Residues n_residues	155
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	65.8 Å
Rg (real space) rg_real	18.50 Å
Rg uncertainty (real space) rg_real_error	0.55 Å
I(0) (real space) i0_real	6.7060e+06
I(0) uncertainty (real space) i0_real_error	9.1850e+04
Rg (reciprocal space) rg_reciprocal	18.49 Å
I(0) (reciprocal space) i0_reciprocal	6706000.0000
Solution quality estimate total_estimate	0.8378
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	19.8 Å
Skewness Skewness skewness	0.503
Kurtosis Kurtosis kurtosis	-0.094
Angular range angular_range	— – 0.4300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	1210000.0000
Real-space data points n_real_points	74
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.679; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.883; Smooth: 0.967

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Anti-silencing protein 1
Molecular weight formula_weight	17499.7 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1402

GASIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELDSILVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEYDEEELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWD

来源 Source

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	4932
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	BROMIDE ION
Molecular weight formula_weight	79.9 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	158

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1roca1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.22 — ASF1-like
Family Family family	b.1.22.1 — ASF1-like

Domain ID domain_id	d1roca2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id	1rocA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1490 — Histone chaperone ASF1-like

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8. Citations (1)

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Unit-cell length a length_a	94.395 Å
Unit-cell length b length_b	31.702 Å
Unit-cell length c length_c	53.625 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	124.55 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.500 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2001
R_work r_work	0.1977
R_free r_free	0.2465

fit	/app/data/saxs_computation/ro/1roc/1roc.fit
pddf	/app/data/pr_computation/ro/1roc/1roc.pr.out
profile	/app/data/saxs_computation/ro/1roc/1roc.dat

Crystal structure of the histone deposition protein Asf1

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

Anti-silencing protein 1

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction