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2nsa

Structures of and interactions between domains of trigger factor from Themotoga maritim

Method: X-RAY DIFFRACTION Dmax: 61.6 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Trigger factor

Thermotoga maritima

UniProt Q9WZF8

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 244–405 Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 7.4；293 K；1.35M ammonium sulfate 0.05M TrisCl, pH 7.4, VAPOR DIFFUSION, temperature 293K Resolution 1.70 Å R-free 0.252
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 244–405 Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 7.4；293 K；1.35M ammonium sulfate 0.05M TrisCl, pH 7.4, VAPOR DIFFUSION, temperature 293K Resolution 1.70 Å R-free 0.252

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 2NSA Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2NSB Structures of and interactions between domains of trigger factor from Themotoga maritima Deposited 2006-11-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–109（109 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；293 K；14% PEG 4000, 0.2M potassium chloride 0.2M, 0.1M MES, pH 6.5, VAPOR DIFFUSION, temperature 293K
Resolution 3.20 Å R-free 0.262
2NSB Structures of and interactions between domains of trigger factor from Themotoga maritima Deposited 2006-11-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–109（109 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；293 K；14% PEG 4000, 0.2M potassium chloride 0.2M, 0.1M MES, pH 6.5, VAPOR DIFFUSION, temperature 293K
Resolution 3.20 Å R-free 0.262
2NSC Structures of and interactions between domains of trigger factor from Themotoga maritima Deposited 2006-11-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–109（109 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；293 K；15% PEG 4000, 0.2M potassium chloride, 0.1M MES, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 6.50
Resolution 2.20 Å R-free 0.260
2NSC Structures of and interactions between domains of trigger factor from Themotoga maritima Deposited 2006-11-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–109（109 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；293 K；15% PEG 4000, 0.2M potassium chloride, 0.1M MES, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 6.50
Resolution 2.20 Å R-free 0.260
3GTY Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone Deposited 2009-03-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain X 1–425（425 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；5-10 % PEG4000, 100 NaOAc, pH 5.5, vapor diffusion, hanging drop, temperature 298K
Resolution 3.40 Å R-free 0.329
3GTY Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone Deposited 2009-03-28 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain X 1–425（425 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；5-10 % PEG4000, 100 NaOAc, pH 5.5, vapor diffusion, hanging drop, temperature 298K
Resolution 3.40 Å R-free 0.329
3GU0 Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone Deposited 2009-03-28 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–405（405 aa） Fragment：residues 1-405
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；10-15% PEG4000, 200 MgCl2, 100 Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 3.50 Å R-free 0.358
6J0A Crystal structure of E. coli methionine aminopeptidase enzyme and chaperone trigger factor fitted into the cryo-EM density map of the complex Deposited 2018-12-22 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 × 2 PDB declaration: dimeric
Chain Q 1–405（405 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 14.20 Å

5 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TIG_THEMA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–163； UniProt 244–405

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 2nsa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2nsa
Deposition date deposition_date2006-11-03
Structure title titleStructures of and interactions between domains of trigger factor from Themotoga maritim
Keywords keywordschaperone; CHAPERONE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier20.37 Å
Radius of gyration Rg (electron density) rg_electron19.14 Å
Forward intensity I(0) i08082630.00
Molecular weight molecular_weight20344.0 kDa
Excluded volume excluded_volume25230 ų
Envelope volume envelope_volume32819 ų
Hydration-shell volume shell_volume15028 ų
Envelope diameter envelope_diameter60.5 Å
Shell Rg shell_rg24.34 Å
Envelope Rg envelope_rg18.88 Å
Shape Rg shape_rg19.17 Å
Total Rg total_rg19.91 Å
Total atoms total_atoms1421
Residues n_residues165
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 dmax61.6 Å
Rg (real space) rg_real20.26 Å
Rg uncertainty (real space) rg_real_error0.39 Å
I(0) (real space) i0_real8.0830e+06
I(0) uncertainty (real space) i0_real_error1.1330e+05
Rg (reciprocal space) rg_reciprocal20.28 Å
I(0) (reciprocal space) i0_reciprocal8083000.0000
Solution quality estimate total_estimate0.9132
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.8 Å
Skewness Skewness skewness-0.000
Kurtosis Kurtosis kurtosis-0.703
Angular range angular_range— – 0.3900 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha926500.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.956; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.999
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2nsaA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology3120 — Trigger factor, domain 2
Homologous superfamily homologous superfamily10 — Trigger factor, C-terminal domain
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8. Citations (1)

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9. Files and Curves (10)