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1k0s

Solution structure of the chemotaxis protein CheW from the thermophilic organism Thermotoga maritima

Method: SOLUTION NMR Dmax: 62.3 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CHEMOTAXIS PROTEIN CHEW

Thermotoga maritima

UniProt Q56311

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 1–151 Fragment：CheW No other associated polymer SOLUTION NMR NMR measurement conditions：pH 4.5；308 K；Ionic strength (raw mmCIF value) 50mM KCl；Pressure 1 NMR sample composition：1mM TMW U-15N,13C; 50mM Acetate buffer | 93% H2O/7% 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 1K0S Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2CH4 Complex between Bacterial Chemotaxis histidine kinase CheA domains P4 and P5 and receptor-adaptor protein CheW Deposited 2006-03-10 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 W 1–151（151 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions PEG 4K 3-5%,NA ACETATE 0.1M PH 4.5,ADPNP 1MM
Resolution 3.50 Å R-free 0.295
2CH4 Complex between Bacterial Chemotaxis histidine kinase CheA domains P4 and P5 and receptor-adaptor protein CheW Deposited 2006-03-10 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 Y 1–151（151 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions PEG 4K 3-5%,NA ACETATE 0.1M PH 4.5,ADPNP 1MM
Resolution 3.50 Å R-free 0.295
3UR1 The structure of a ternary complex between CheA domains P4 and P5 with CheW and with a truncated fragment of TM14, a chemoreceptor analog from Thermotoga maritima. Deposited 2011-11-21 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 9–147（139 aa） Fragment：unp residues 9-147
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 8.5；293 K；0.2 M sodium acetate trihydrate, 0.1 M Tris, 15% w/v Polyethylene glycol 4,000, pH 8.5, EVAPORATION, temperature 293K
Resolution 4.50 Å R-free 0.291
4JPB The structure of a ternary complex between CheA domains P4 and P5 with CheW and with an unzipped fragment of TM14, a chemoreceptor analog from Thermotoga maritima. Deposited 2013-03-19 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain W 1–147（147 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；Cubic shaped crystals (50x50x50 um3) were grown from a mixture of 520 uM Tm14s, 457 uM CheA 354 and 121 uM CheW after 1 month by vapor diffusion from a 2 ul drop (1:1 mixture of protein and reservoir: 500 ul reservoir of 0.2 M sodium acetate trihydrate, 0.1 M Tris (pH 8.5), 15% w/v polyethylene glycol 4,000), VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 3.19 Å R-free 0.220

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHEW_THEMA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–151； UniProt 1–151

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 1k0s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1k0s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1k0s
Deposition date deposition_date2001-09-20
Structure title titleSolution structure of the chemotaxis protein CheW from the thermophilic organism Thermotoga maritima
Keywords keywordsCheW, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier16.19 Å
Radius of gyration Rg (electron density) rg_electron15.69 Å
Forward intensity I(0) i01382520000.00
Molecular weight molecular_weight338680.0 kDa
Excluded volume excluded_volume434340 ų
Envelope volume envelope_volume46270 ų
Hydration-shell volume shell_volume19952 ų
Envelope diameter envelope_diameter70.4 Å
Shell Rg shell_rg26.35 Å
Envelope Rg envelope_rg20.46 Å
Shape Rg shape_rg15.64 Å
Total Rg total_rg16.10 Å
Total atoms total_atoms49100
Residues n_residues3020
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 dmax62.3 Å
Rg (real space) rg_real16.16 Å
Rg uncertainty (real space) rg_real_error0.58 Å
I(0) (real space) i0_real1.3830e+09
I(0) uncertainty (real space) i0_real_error1.8450e+07
Rg (reciprocal space) rg_reciprocal16.17 Å
I(0) (reciprocal space) i0_reciprocal1383000000.0000
Solution quality estimate total_estimate0.6947
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.6 Å
Skewness Skewness skewness0.356
Kurtosis Kurtosis kurtosis0.040
Angular range angular_range— – 0.4900 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha842500.0000
Real-space data points n_real_points79
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.373; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.907; 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 (1 domains)

Domain ID domain_idd1k0sa_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.7 — CheW-like
Family Family familyb.40.7.1 — CheW-like

CATH v4.4 (2 domains)

Domain ID domain_id1k0sA01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains
Domain ID domain_id1k0sA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily180 — CheA-289, Domain 4
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8. Citations (1)

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9. Files and Curves (10)