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2mnj

NMR solution structure of the yeast Pih1 and Tah1 C-terminal domains complex

Method: SOLUTION NMR Dmax: 53.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

TPR repeat-containing protein associated with Hsp90

Saccharomyces cerevisiae

UniProt P25638

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 93–111 Fragment：UNP residues 93-111 Protein interacting with Hsp90 1 × 1 （P38768） 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

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 2MNJ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2L6J Tah1 complexed by MEEVD Deposited 2010-11-22 Different construct Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–111（111 aa）
Not recorded No recorded non-water small molecule 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
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
4CGQ Full length Tah1 bound to HSP90 peptide SRMEEVD Deposited 2013-11-26 Different construct 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 construct 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 5–23； UniProt 93–111

Protein interacting with Hsp90 1

Saccharomyces cerevisiae

UniProt P38768

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 B； UniProt 257–344 Fragment：UNP residues 257-344 TPR repeat-containing protein associated with Hsp90 × 1 （P25638） 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

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 2MNJ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
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 experimental method Different experimental conditions 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
4CHH N-terminal domain of yeast PIH1p Deposited 2013-12-02 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–185（185 aa） Fragment：N-TERMINUS, RESIDUES 1-185
Not recorded EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7
Resolution 2.03 Å R-free 0.237
4CHH N-terminal domain of yeast PIH1p Deposited 2013-12-02 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–185（185 aa） Fragment：N-TERMINUS, RESIDUES 1-185
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7
Resolution 2.03 Å R-free 0.237

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PIH1_YEAST
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 1–88； UniProt 257–344

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

SAXS profile for 2mnj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2mnj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2mnj
Deposition date deposition_date2014-04-08
Structure title titleNMR solution structure of the yeast Pih1 and Tah1 C-terminal domains complex
Keywords keywordsCS-domain, R2TP, HSP90, snoRNP assembly, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.39 Å
Radius of gyration Rg (electron density) rg_electron14.68 Å
Forward intensity I(0) i0856681000.00
Molecular weight molecular_weight258620.0 kDa
Excluded volume excluded_volume327870 ų
Envelope volume envelope_volume30150 ų
Hydration-shell volume shell_volume15066 ų
Envelope diameter envelope_diameter60.6 Å
Shell Rg shell_rg23.16 Å
Envelope Rg envelope_rg18.32 Å
Shape Rg shape_rg14.67 Å
Total Rg total_rg14.85 Å
Total atoms total_atoms36820
Residues n_residues2220
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax53.4 Å
Rg (real space) rg_real15.38 Å
Rg uncertainty (real space) rg_real_error0.42 Å
I(0) (real space) i0_real8.5670e+08
I(0) uncertainty (real space) i0_real_error1.0580e+07
Rg (reciprocal space) rg_reciprocal15.38 Å
I(0) (reciprocal space) i0_reciprocal856700000.0000
Solution quality estimate total_estimate0.7820
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary16.9 Å
Skewness Skewness skewness0.299
Kurtosis Kurtosis kurtosis-0.260
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha330700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.741; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.941; 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_id2mnjB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily4160 —
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8. Citations (1)

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9. Files and Curves (10)