4nq0

Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones

Method: X-RAY DIFFRACTION D_max: 72.4 Å Quality: GOOD

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

HAT1-interacting factor 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 1–385	Fragment：HAT1-interacting factor 1	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6；287 K；0.1M sodium cacodylate, 15% PEG4000, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 287K	Resolution 2.10 Å R-free 0.243

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 4NQ0	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5BT1 histone chaperone Hif1 playing with histone H2A-H2B dimer Deposited 2015-06-02	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–385（385 aa） Chain B 1–385（385 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；287 K；0.1M Magnesium formate dihydrate, 15% PEG3350	Resolution 2.62 Å R-free 0.262

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

View Construct and Data Evidence

UniProt name	HIF1_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–385； UniProt 1–385

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	4nq0
Deposition date deposition_date	2013-11-23
Structure title title	Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones
Keywords keywords	TPR, NASP homologue, SHNi-TPR, mediating protein-protein interactions, histone chaperone, Nucleus, CHAPERONE; 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	20.61 Å
Radius of gyration Rg (electron density) rg_electron	19.58 Å
Forward intensity I(0) i0	14899500.00
Molecular weight molecular_weight	28696.0 kDa
Excluded volume excluded_volume	35794 Å³
Envelope volume envelope_volume	42860 Å³
Hydration-shell volume shell_volume	18585 Å³
Envelope diameter envelope_diameter	74.3 Å
Shell Rg shell_rg	25.59 Å
Envelope Rg envelope_rg	19.85 Å
Shape Rg shape_rg	19.57 Å
Total Rg total_rg	20.48 Å
Total atoms total_atoms	2022
Residues n_residues	254
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	72.4 Å
Rg (real space) rg_real	20.58 Å
Rg uncertainty (real space) rg_real_error	0.64 Å
I(0) (real space) i0_real	1.4900e+07
I(0) uncertainty (real space) i0_real_error	1.7680e+05
Rg (reciprocal space) rg_reciprocal	20.59 Å
I(0) (reciprocal space) i0_reciprocal	14900000.0000
Solution quality estimate total_estimate	0.7844
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	25.2 Å
Skewness Skewness skewness	0.326
Kurtosis Kurtosis kurtosis	-0.226
Angular range angular_range	— – 0.3850 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4252000.0000
Real-space data points n_real_points	70
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.745; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	4nq0A00
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	10 — Tetratricopeptide repeat domain

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8. Citations (1)

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Unit-cell length a length_a	48.308 Å
Unit-cell length b length_b	78.280 Å
Unit-cell length c length_c	82.689 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	41.300 Å
R factor r_factor	0.2127
R_work r_work	0.2111
R_free r_free	0.2430

Description description	HAT1-interacting factor 1
Molecular weight formula_weight	44553.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2089

Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones

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

HAT1-interacting factor 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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Saccharomyces cerevisiae
通用名 common_name	;Baker's yeast ;
NCBI Class编号 ncbi_taxonomy_id	559292
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	67

fit	/app/data/saxs_computation/nq/4nq0/4nq0.fit
pddf	/app/data/pr_computation/nq/4nq0/4nq0.pr.out
profile	/app/data/saxs_computation/nq/4nq0/4nq0.dat