2lsv

The NMR high resolution structure of yeast Tah1 in complex with the Hsp90 C-terminal tail

Method: SOLUTION NMR Dmax: 35.8 Å Quality: REASONABLE

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 2–111 Not recorded ATP-dependent molecular chaperone HSP82 × 1 (P02829) 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

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.

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 1–110; UniProt 2–111

ATP-dependent molecular chaperone HSP82

OrganismNot specified

UniProt P02829

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 701–709 Fragment:C-terminal tail TPR repeat-containing protein associated with Hsp90 × 1 (P25638) 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

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.

47 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HSP82_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–9; UniProt 701–709

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 2lsv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2lsv
Deposition date deposition_date2012-05-07
Structure title titleThe NMR high resolution structure of yeast Tah1 in complex with the Hsp90 C-terminal tail
Keywords keywordsCHAPERONE-BINDING PROTEIN-CHAPERONE complex; CHAPERONE-BINDING PROTEIN/CHAPERONE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.92
Radius of gyration Rg (electron density) rg_electron17.95
Forward intensity I(0) i01083060000.00
Molecular weight molecular_weight268240.0 kDa
Excluded volume excluded_volume331750 ų
Envelope volume envelope_volume80300 ų
Hydration-shell volume shell_volume24497 ų
Envelope diameter envelope_diameter86.0
Shell Rg shell_rg34.15
Envelope Rg envelope_rg30.77
Shape Rg shape_rg17.99
Total Rg total_rg18.24
Total atoms total_atoms37200
Residues n_residues2380
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

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

Maximum dimension Dmax dmax35.8
Rg (real space) rg_real13.11
Rg uncertainty (real space) rg_real_error0.04
I(0) (real space) i0_real8.7460e+08
I(0) uncertainty (real space) i0_real_error6.7480e+06
Rg (reciprocal space) rg_reciprocal18.50
I(0) (reciprocal space) i0_reciprocal1083000000.0000
Solution quality estimate total_estimate0.6044
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary17.4
Skewness Skewness skewness0.191
Kurtosis Kurtosis kurtosis-0.410
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha5.1310
Highest regularization parameter α highest_alpha389500.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.122; Oscil: 0.988; Stabil: 0.966; Sysdev: 0.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2lsvA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain

8. Citations (1)

9. Files and Curves (10)