SAXSdb — 4chh

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

PROTEIN INTERACTING WITH HSP90 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 1–185	Fragment：N-TERMINUS, RESIDUES 1-185	EDO 1,2-ETHANEDIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7；pH 7	Resolution 2.03 Å R-free 0.237
2	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain B； UniProt 1–185	Fragment：N-TERMINUS, RESIDUES 1-185	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7；pH 7	Resolution 2.03 Å R-free 0.237

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 4CHH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2MNJ NMR solution structure of the yeast Pih1 and Tah1 C-terminal domains complex Deposited 2014-04-08	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 257–344（88 aa） Fragment：UNP residues 257-344	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.4；298 K；Ionic strength (raw mmCIF value) 50；Pressure ambient NMR sample composition 1.5 mM [U-99% 13C; U-99% 15N] Tah1, 1.5 mM [U-99% 13C; U-99% 15N] Pih1, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
4CGU Full length Tah1 bound to yeast PIH1 and HSP90 peptide SRMEEVD Deposited 2013-11-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 187–344（158 aa） Fragment：C-TERMINAL DOMAIN, RESIDUES 187-344	Non-standard monomer：Yes (specific site not provided by mmCIF)	GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7	Resolution 2.11 Å R-free 0.210

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PIH1_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–185； UniProt 1–185 Author chain B； PDBConstruct 1–185； UniProt 1–185

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	4chh
Deposition date deposition_date	2013-12-02
Structure title title	N-terminal domain of yeast PIH1p
Keywords keywords	CHAPERONE, R2TP, TAH1; 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	23.24 Å
Radius of gyration Rg (electron density) rg_electron	22.41 Å
Forward intensity I(0) i0	21737000.00
Molecular weight molecular_weight	35289.0 kDa
Excluded volume excluded_volume	44244 Å³
Envelope volume envelope_volume	54675 Å³
Hydration-shell volume shell_volume	21205 Å³
Envelope diameter envelope_diameter	73.6 Å
Shell Rg shell_rg	28.23 Å
Envelope Rg envelope_rg	22.60 Å
Shape Rg shape_rg	22.41 Å
Total Rg total_rg	23.24 Å
Total atoms total_atoms	4868
Residues n_residues	315
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	75.7 Å
Rg (real space) rg_real	23.29 Å
Rg uncertainty (real space) rg_real_error	0.57 Å
I(0) (real space) i0_real	2.1740e+07
I(0) uncertainty (real space) i0_real_error	3.2140e+05
Rg (reciprocal space) rg_reciprocal	23.28 Å
I(0) (reciprocal space) i0_reciprocal	21740000.0000
Solution quality estimate total_estimate	0.8883
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	23.3 Å
Skewness Skewness skewness	0.392
Kurtosis Kurtosis kurtosis	-0.408
Angular range angular_range	— – 0.3400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	8427000.0000
Real-space data points n_real_points	66
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.880; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.945

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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	PROTEIN INTERACTING WITH HSP90 1
Molecular weight formula_weight	21452.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	5151

MADFLLRPIKQRHRNEDKYVSVDAADGSVSKIEPIADFVIKTKLLSANGPEKLQDGRKVFINVCHSPLVPKPEVDFNARIVFPLIIQNEWEIPIITSCYRMDHDKKGQECYVWDCCINSDCSRWICDDIQLREILVEWCLESCEIRDSVVLCRDRIAFPKMKKKGAELPALEVLNDELHQDYKAK

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	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	249

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8. Citations (1)

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Unit-cell length a length_a	39.750 Å
Unit-cell length b length_b	48.290 Å
Unit-cell length c length_c	96.280 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	98.10 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.030 Å
Low-resolution limit resolution_low	47.660 Å
R factor r_factor	0.1880
R_work r_work	0.1855
R_free r_free	0.2367

fit	/app/data/saxs_computation/ch/4chh/4chh.fit
pddf	/app/data/pr_computation/ch/4chh/4chh.pr.out
profile	/app/data/saxs_computation/ch/4chh/4chh.dat

N-terminal domain of yeast PIH1p

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

PROTEIN INTERACTING WITH HSP90 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