1egs

NMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURES

Method: SOLUTION NMR Dmax: 14.6 Å Quality: GOOD

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

GROES

Escherichia coli

UniProt P0A6F9

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 19–27 Fragment:MOBILE LOOP Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;303 K 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.

28 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CH10_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–10; UniProt 19–27

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 1egs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1egs
Deposition date deposition_date1997-06-30
Structure title titleNMR STRUCTURE OF GROES MOBILE LOOP RESIDUES 19-27 IN THE SYNTHETIC PEPTIDE (RESIDUES 13-32) BOUND TO GROEL, 20 STRUCTURES
Keywords keywordsCHAPERONIN, PROTEIN FOLDING, HEAT SHOCK; CHAPERONIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier4.46
Radius of gyration Rg (electron density) rg_electron5.28
Forward intensity I(0) i03930640.00
Molecular weight molecular_weight17762.0 kDa
Excluded volume excluded_volume23104 ų
Envelope volume envelope_volume1808 ų
Hydration-shell volume shell_volume3065 ų
Envelope diameter envelope_diameter17.9
Shell Rg shell_rg10.14
Envelope Rg envelope_rg6.11
Shape Rg shape_rg5.22
Total Rg total_rg5.82
Total atoms total_atoms2680
Residues n_residues180
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 dmax14.6
Rg (real space) rg_real4.46
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real3.9310e+06
I(0) uncertainty (real space) i0_real_error3.4890e+04
Rg (reciprocal space) rg_reciprocal4.46
I(0) (reciprocal space) i0_reciprocal3931000.0000
Solution quality estimate total_estimate0.7883
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary5.5
Skewness Skewness skewness0.043
Kurtosis Kurtosis kurtosis-1.230
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha137.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 0.964; Sysdev: 1.000; Positv: 1.000; Valcen: 0.789; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1egsa_
Class classj — Peptides
Fold Fold foldj.50 — GroES fragments
Superfamily Superfamily superfamilyj.50.1 — GroES fragments
Family Family familyj.50.1.1 — GroES fragments

8. Citations (2)

9. Files and Curves (10)