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1bq0

J-DOMAIN (RESIDUES 1-77) OF THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 1-104) OF THE MOLECULAR CHAPERONE DNAJ, NMR, 20 STRUCTURES

Method: SOLUTION NMR Dmax: 51.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

DNAJ

Escherichia coli

UniProt P08622

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 1–103 Fragment：N-TERMINAL FRAGMENT (RESIDUES 1-104) No other associated polymer SOLUTION NMR NMR measurement conditions：pH 6；303 K；Ionic strength (raw mmCIF value) 50 mM PHOSPHATE NMR sample composition：2MM, 10% D2O IN H2O 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 1BQ0 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BQZ J-DOMAIN (RESIDUES 1-77) OF THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 1-78) OF THE MOLECULAR CHAPERONE DNAJ, NMR, 20 STRUCTURES Deposited 1998-08-20 Different construct Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–77（77 aa） Fragment：N-TERMINAL FRAGMENT (RESIDUES 1-78)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；303 K；Ionic strength (raw mmCIF value) 50 mM PHOSPHATE
NMR sample composition 2MM, 10% D2O IN H2O
Resolution not provided
1EXK SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE ESCHERICHIA COLI CHAPERONE PROTEIN DNAJ. Deposited 2000-05-03 Different construct Different ligand/ion Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 131–209（79 aa） Fragment：RESIDUES 131-209
Not recorded ZN ZINC ION × 2 SOLUTION NMR
NMR measurement conditions pH 6.8；293 K；Ionic strength (raw mmCIF value) 50 mM；Pressure 1
NMR measurement conditions pH 6.8；293 K；Ionic strength (raw mmCIF value) 50 mM；Pressure 1
NMR sample composition 600 uM DnaJ CRD U-15N,13C; 20 mM Tris-d11 pH 6.8; 300 uM ZnCl2; 50 mM NaCl; 2 mM DTT; 0.02% NaN3 | 95% H2O/5% D2O
NMR sample composition 600 uM DnaJ CRD U-15N; 20 mM Tris-d11 pH 6.8; 300 uM ZnCl2; 50 mM NaCl; | 95% H2O/5% D2O
Resolution not provided
1XBL NMR STRUCTURE OF THE J-DOMAIN (RESIDUES 2-76) IN THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 2-108) OF THE MOLECULAR CHAPERONE DNAJ, 20 STRUCTURES Deposited 1996-10-07 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–107（107 aa） Fragment：N-TERMINAL FRAGMENT (RESIDUES 2-108) OF THE MOLECULAR CHAPERONE DNAJ
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；301 K
Resolution not provided
5NRO Structure of full-length DnaK with bound J-domain Deposited 2017-04-25 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 B 1–105（105 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；9% w/v PEG 8000 0.1M calcium acetate 0.1 M imidazole pH 6.5 protein at 18 mg/ml crystalization drop contained 200 nl protein + 100 nl reservoir solution
Resolution 3.25 Å R-free 0.234

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

View Construct and Data Evidence
UniProt name DNAJ_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–103； UniProt 1–103

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 1bq0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bq0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bq0
Deposition date deposition_date1998-08-20
Structure title titleJ-DOMAIN (RESIDUES 1-77) OF THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 1-104) OF THE MOLECULAR CHAPERONE DNAJ, NMR, 20 STRUCTURES
Keywords keywordsCHAPERONE, HEAT SHOCK, PROTEIN FOLDING, DNAK; 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_guinier13.92 Å
Radius of gyration Rg (electron density) rg_electron13.39 Å
Forward intensity I(0) i0481295000.00
Molecular weight molecular_weight179220.0 kDa
Excluded volume excluded_volume221740 ų
Envelope volume envelope_volume27115 ų
Hydration-shell volume shell_volume14307 ų
Envelope diameter envelope_diameter55.2 Å
Shell Rg shell_rg21.87 Å
Envelope Rg envelope_rg16.84 Å
Shape Rg shape_rg13.35 Å
Total Rg total_rg13.70 Å
Total atoms total_atoms24899
Residues n_residues1540
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 dmax51.0 Å
Rg (real space) rg_real13.95 Å
Rg uncertainty (real space) rg_real_error0.40 Å
I(0) (real space) i0_real4.8130e+08
I(0) uncertainty (real space) i0_real_error5.1730e+06
Rg (reciprocal space) rg_reciprocal13.95 Å
I(0) (reciprocal space) i0_reciprocal481300000.0000
Solution quality estimate total_estimate0.8302
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.2 Å
Skewness Skewness skewness0.340
Kurtosis Kurtosis kurtosis-0.333
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha234700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.681; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.757; Smooth: 0.990
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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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bq0a_
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.3 — Chaperone J-domain
Family Family familya.2.3.1 — Chaperone J-domain

CATH v4.4 (1 domains)

Domain ID domain_id1bq0A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily110 — DnaJ domain
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8. Citations (2)

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9. Files and Curves (10)