2lo1

NMR structure of the protein BC008182, a DNAJ-like domain from Homo sapiens

Method: SOLUTION NMR Dmax: 45.3 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

DnaJ homolog subfamily A member 1

Homo sapiens

UniProt P31689

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 1–70 Fragment:J domain residues 1-70 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;298 K;Ionic strength (raw mmCIF value) 0.080;Pressure ambient NMR sample composition:1.2 mM [U-98% 13C; U-98% 15N] protein, 20 mM sodium phosphate, 5 mM sodium azide, 50 mM sodium chloride, 95 % H2O, 5 % D2O, 95% H2O/5% D2O | 95% H2O/5% 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DNJA1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–71; UniProt 1–70

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 2lo1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lo1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2lo1
Deposition date deposition_date2012-01-09
Structure title titleNMR structure of the protein BC008182, a DNAJ-like domain from Homo sapiens
Keywords keywordsCHAPERONE, PSI-Biology, Joint Center for Structural Genomics, JCSG, Partnership for Stem Cell Biology, STEMCELL; CHAPERONE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.28
Radius of gyration Rg (electron density) rg_electron13.07
Forward intensity I(0) i0366574000.00
Molecular weight molecular_weight163890.0 kDa
Excluded volume excluded_volume206090 ų
Envelope volume envelope_volume19789 ų
Hydration-shell volume shell_volume11850 ų
Envelope diameter envelope_diameter49.5
Shell Rg shell_rg19.86
Envelope Rg envelope_rg14.90
Shape Rg shape_rg12.99
Total Rg total_rg13.51
Total atoms total_atoms23160
Residues n_residues1420
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 dmax45.3
Rg (real space) rg_real13.27
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real3.6660e+08
I(0) uncertainty (real space) i0_real_error4.1570e+06
Rg (reciprocal space) rg_reciprocal13.27
I(0) (reciprocal space) i0_reciprocal366600000.0000
Solution quality estimate total_estimate0.8786
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.5
Skewness Skewness skewness0.220
Kurtosis Kurtosis kurtosis-0.437
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha75370.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.820; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.966; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2lo1a1
Class classa — All alpha proteins
Fold Fold folda.2 — Long alpha-hairpin
Superfamily Superfamily superfamilya.2.3 — Chaperone J-domain
Family Family familya.2.3.0 — automated matches
Domain ID domain_idd2lo1a2
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_id2lo1A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily110 — DnaJ domain

8. Citations (1)

9. Files and Curves (10)