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2lni

Solution NMR Structure of Stress-induced-phosphoprotein 1 STI1 from Homo sapiens, Northeast Structural Genomics Consortium Target HR4403E

Method: SOLUTION NMR Dmax: 46.4 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Stress-induced-phosphoprotein 1

Homo sapiens

UniProt P31948

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 356–477 Fragment：TPR repeats 7-9, residues 356-477 No other associated polymer SOLUTION NMR NMR measurement conditions：pH 4.5；293 K；Pressure ambient NMR sample composition：0.807 mM [U-100% 13C; U-100% 15N] HR4403E, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition：0.763 mM [U-5% 13C; U-100% 15N] HR4403E, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition：0.4 mM [U-100% 13C; U-100% 15N] HR4403E, 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 2LNI Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1ELR Crystal structure of the TPR2A domain of HOP in complex with the HSP90 peptide MEEVD Deposited 2000-03-14 Different construct Different oligomeric state 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 222–352（131 aa） Fragment：MIDDLE DOMAIN
Not recorded NI NICKEL (II) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；PEG MME 2000, TRIS, Nickel chloride, Xylitol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.90 Å R-free 0.219
1ELW Crystal structure of the TPR1 domain of HOP in complex with a HSC70 peptide Deposited 2000-03-14 Different construct Different oligomeric state 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 1–118（118 aa） Fragment：N-TERMINAL DOMAIN
Not recorded NI NICKEL (II) ION × 2 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；PEG MME 2000, TRIS, Nickel Chloride, Xylitol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.60 Å R-free 0.215
1ELW Crystal structure of the TPR1 domain of HOP in complex with a HSC70 peptide Deposited 2000-03-14 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–118（118 aa） Fragment：N-TERMINAL DOMAIN
Not recorded NI NICKEL (II) ION × 2 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；PEG MME 2000, TRIS, Nickel Chloride, Xylitol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.60 Å R-free 0.215
2NC9 Apo solution structure of Hop TPR2A Deposited 2016-03-23 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 220–350（131 aa） Fragment：residues 280-350
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 70；Pressure ambient
NMR sample composition 1.5 mM [U-13C; U-15N] protein, 20 mM sodium phosphate, 50 mM sodium chloride, 1 mM DTT, 0.01 % sodium azide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.5 mM [U-13C; U-15N] protein, 20 mM sodium phosphate, 50 mM sodium chloride, 1 mM DTT, 0.01 % sodium azide, 100% D2O | 100% D2O
Resolution not provided
3ESK Structure of HOP TPR2A domain in complex with the non-cognate Hsc70 peptide ligand Deposited 2008-10-06 Different construct Different oligomeric state 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 222–349（128 aa） Fragment：TPR2A domain, UNP residues 223-350
Not recorded NI NICKEL (II) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；298 K；TRIS pH 8.5, PEG MME 2000, NiCl2, Xylitol, VAPOR DIFFUSION, temperature 298K
Resolution 2.05 Å R-free 0.244
3FWV Crystal Structure of a Redesigned TPR Protein, T-MOD(VMY), in Complex with MEEVF Peptide Deposited 2009-01-19 Different construct Different oligomeric state 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 223–349（127 aa） Fragment：TPR repeats 4-6
Not recorded NI NICKEL (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；100 mM Tris pH 8.5, 30% PEG MME 2000, 5-10 mM NiCl2, 10% xylitol, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.20 Å R-free 0.244
3FWV Crystal Structure of a Redesigned TPR Protein, T-MOD(VMY), in Complex with MEEVF Peptide Deposited 2009-01-19 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 223–349（127 aa） Fragment：TPR repeats 4-6
Not recorded NI NICKEL (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；100 mM Tris pH 8.5, 30% PEG MME 2000, 5-10 mM NiCl2, 10% xylitol, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.20 Å R-free 0.244
7KW7 Atomic cryoEM structure of Hsp90-Hsp70-Hop-GR Deposited 2020-11-30 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain E 1–543（543 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 K POTASSIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.57 Å
9QQU Crystal structure of an engineered TPR domain in complex with the HSP90 peptide MEEVD Deposited 2025-04-02 Different construct Different oligomeric state 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 218–350（133 aa）
Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5；293 K；0.1M Sodium Acetate, pH 5.0 2.0 M Ammonium sulphate
Resolution 2.13 Å R-free 0.256

7 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STIP1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 12–133； UniProt 356–477

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 2lni

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2lni
Deposition date deposition_date2011-12-28
Structure title titleSolution NMR Structure of Stress-induced-phosphoprotein 1 STI1 from Homo sapiens, Northeast Structural Genomics Consortium Target HR4403E
Keywords keywordsStructural Genomics, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG), PSI-BIOLOGY, Protein Structure Initiative, CHAPERONE; CHAPERONE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier17.53 Å
Radius of gyration Rg (electron density) rg_electron17.28 Å
Forward intensity I(0) i01437090000.00
Molecular weight molecular_weight306810.0 kDa
Excluded volume excluded_volume377950 ų
Envelope volume envelope_volume57072 ų
Hydration-shell volume shell_volume21265 ų
Envelope diameter envelope_diameter81.7 Å
Shell Rg shell_rg29.51 Å
Envelope Rg envelope_rg25.13 Å
Shape Rg shape_rg17.27 Å
Total Rg total_rg17.55 Å
Total atoms total_atoms42360
Residues n_residues2660
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 dmax46.4 Å
Rg (real space) rg_real16.32 Å
Rg uncertainty (real space) rg_real_error0.07 Å
I(0) (real space) i0_real1.3660e+09
I(0) uncertainty (real space) i0_real_error1.1380e+07
Rg (reciprocal space) rg_reciprocal17.73 Å
I(0) (reciprocal space) i0_reciprocal1437000000.0000
Solution quality estimate total_estimate0.6872
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary19.2 Å
Skewness Skewness skewness0.257
Kurtosis Kurtosis kurtosis-0.530
Angular range angular_range— – 0.4550 Å−1
Current regularization parameter α current_alpha3.4230
Highest regularization parameter α highest_alpha442400.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.008; Oscil: 1.000; Stabil: 0.983; Sysdev: 0.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2lnia1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.8 — TPR-like
Family Family familya.118.8.0 — automated matches
Domain ID domain_idd2lnia2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2lniA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain
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8. Citations (1)

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9. Files and Curves (10)