SAXSdb — 2l6j

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

TPR repeat-containing protein associated with Hsp90

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–111	Not recorded	C-terminus Hsp90 chaperone peptide MEEVD × 1	SOLUTION NMR NMR measurement conditions：pH 8；293 K；Ionic strength (raw mmCIF value) 0.1375；Pressure ambient NMR sample composition：1 mM [U-99% 15N] Tah1-1, 2 mM Ac-MEEVD-2, 25 mM sodium phosphate-3, 100 mM sodium chloride-4, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：1 mM [U-99% 13C; U-99% 15N] Tah1-5, 2 mM Ac-MEEVD-6, 25 mM sodium phosphate-7, 100 mM sodium chloride-8, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：800 uM Tah1-9, 1.6 mM Ac-MEEVD-10, 25 mM sodium phosphate-11, 100 mM sodium chloride-12, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition：1 mM [U-98% 13C; U-98% 15N] Tah1-13, 2 mM Ac-MEEVD-14, 25 mM sodium phosphate-15, 100 mM sodium chloride-16, 100% D2O \| 100% D2O	Resolution not provided

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 2L6J	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2LSU The NMR high resolution structure of yeast Tah1 in a free form Deposited 2012-05-07	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–111（110 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.2；288 K；Ionic strength (raw mmCIF value) 0.15；Pressure ambient NMR sample composition 1 mM [U-100% 13C; U-100% 15N] Tah1, 10 mM sodium phosphate, 150 mM sodium chloride, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 1 mM [U-100% 13C; U-100% 15N] Tah1, 10 mM sodium phosphate, 150 mM sodium chloride, 100% D2O \| 100% D2O	Resolution not provided
2LSV The NMR high resolution structure of yeast Tah1 in complex with the Hsp90 C-terminal tail Deposited 2012-05-07	Different construct Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 2–111（110 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.2；288 K；Ionic strength (raw mmCIF value) 0.15；Pressure ambient NMR sample composition 1 mM [U-100% 13C; U-100% 15N] protein_1, 1 mM protein_2, 10 mM sodium phosphate, 150 mM sodium chloride, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 1 mM [U-100% 13C; U-100% 15N] protein_1, 1 mM protein_2, 10 mM sodium phosphate, 150 mM sodium chloride, 100% D2O \| 100% D2O	Resolution not provided
2MNJ NMR solution structure of the yeast Pih1 and Tah1 C-terminal domains complex Deposited 2014-04-08	Different construct Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 93–111（19 aa） Fragment：UNP residues 93-111	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
4CGQ Full length Tah1 bound to HSP90 peptide SRMEEVD Deposited 2013-11-26	Different mutation/modification 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 1–111（111 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7	Resolution 2.00 Å R-free 0.210
4CGU Full length Tah1 bound to yeast PIH1 and HSP90 peptide SRMEEVD Deposited 2013-11-26	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–111（111 aa）	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

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TAH1_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–111； UniProt 1–111

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	2l6j
Deposition date deposition_date	2010-11-22
Structure title title	Tah1 complexed by MEEVD
Keywords keywords	tetratricopeptide repeat (TPR), Hsp90 co-factor, PROTEIN BINDING; PROTEIN BINDING
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	16.54 Å
Radius of gyration Rg (electron density) rg_electron	16.39 Å
Forward intensity I(0) i0	1024270000.00
Molecular weight molecular_weight	262580.0 kDa
Excluded volume excluded_volume	325570 Å³
Envelope volume envelope_volume	58257 Å³
Hydration-shell volume shell_volume	22095 Å³
Envelope diameter envelope_diameter	68.6 Å
Shell Rg shell_rg	29.29 Å
Envelope Rg envelope_rg	23.67 Å
Shape Rg shape_rg	16.39 Å
Total Rg total_rg	16.67 Å
Total atoms total_atoms	36820
Residues n_residues	2320
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	45.8 Å
Rg (real space) rg_real	15.70 Å
Rg uncertainty (real space) rg_real_error	0.08 Å
I(0) (real space) i0_real	9.8060e+08
I(0) uncertainty (real space) i0_real_error	7.7830e+06
Rg (reciprocal space) rg_reciprocal	16.72 Å
I(0) (reciprocal space) i0_reciprocal	1024000000.0000
Solution quality estimate total_estimate	0.6782
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	17.9 Å
Skewness Skewness skewness	0.451
Kurtosis Kurtosis kurtosis	-0.255
Angular range angular_range	— – 0.4800 Å⁻¹
Current regularization parameter α current_alpha	3.8600
Highest regularization parameter α highest_alpha	492300.0000
Real-space data points n_real_points	78
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.001; Oscil: 0.952; Stabil: 0.988; Sysdev: 0.000; Positv: 1.000; Valcen: 0.994; 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)

Entity 1 Entity 1 polymer

Description description	TPR repeat-containing protein associated with Hsp90
Molecular weight formula_weight	12524.1 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	36820

MSQFEKQKEQGNSLFKQGLYREAVHCYDQLITAQPQNPVGYSNKAMALIKLGEYTQAIQMCQQGLRYTSTAEHVAIRSKLQYRLELAQGAVGSVQIPVVEVDELPEGYDRS

来源 Source

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

Entity 2 Entity 2 polymer

Description description	C-terminus Hsp90 chaperone peptide MEEVD
Molecular weight formula_weight	621.7 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MEEVD

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	2l6jA00
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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fit	/app/data/saxs_computation/l6/2l6j/2l6j.fit
pddf	/app/data/pr_computation/l6/2l6j/2l6j.pr.out
profile	/app/data/saxs_computation/l6/2l6j/2l6j.dat

Tah1 complexed by MEEVD

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

TPR repeat-containing protein associated with Hsp90

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)