1d6k

NMR SOLUTION STRUCTURE OF THE 5S RRNA E-LOOP/L25 COMPLEX

Method: SOLUTION NMR Dmax: 71.2 Å Quality: REASONABLE

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

RIBOSOMAL PROTEIN L25

Escherichia coli

UniProt P68919

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–RNA Monomer Protein × 1 RNA 1 PDB declaration: dimeric(2) Consistent with all polymer counts Chain A; UniProt 1–94 Not recorded 5S RRNA E-LOOP (5SE) × 1 SOLUTION NMR NMR measurement conditions:pH 7.2;298 K;Ionic strength (raw mmCIF value) 100mM KCL;Pressure AMBIENT NMR measurement conditions:pH 7.2;298 K;Ionic strength (raw mmCIF value) 100mM KCL;Pressure AMBIENT NMR measurement conditions:pH 7.2;298 K;Ionic strength (raw mmCIF value) 100mM KCL;Pressure AMBIENT NMR measurement conditions:pH 7.2;298 K;Ionic strength (raw mmCIF value) 100mM KCL;Pressure AMBIENT NMR measurement conditions:pH 7.2;298 K;Ionic strength (raw mmCIF value) 100mM KCL;Pressure AMBIENT NMR measurement conditions:pH 7.2;298 K;Ionic strength (raw mmCIF value) 100mM KCL;Pressure AMBIENT NMR sample composition:2MM L25 U-15N,13C/5SE NA; 20MM PHOSPHATE BUFFER; 100MM KCL NMR sample composition:2.2MM L25 U-15N,13C/5SE NA; 20MM PHOSPHATE BUFFER; 100MM KCL NMR sample composition:1.8MM L25 NA/5SE U-15N; 20MM PHOSPHATE BUFFER; 100MM KCL NMR sample composition:1MM L25 U-15N/5SE U-15N; 20MM PHOSPHATE BUFFER; 100MM KCL NMR sample composition:1.8MM L25 NA/5SE U-15N,13C; 20MM PHOSPHATE BUFFER; 100MM KCL NMR sample composition:1.7MM L25 NA/5SE U-15N,13C; 20MM PHOSPHATE BUFFER; 100MM KCL 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.

478 other PDB entries and 523 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL25_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–94; UniProt 1–94

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 1d6k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1d6k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1d6k
Deposition date deposition_date1999-10-14
Structure title titleNMR SOLUTION STRUCTURE OF THE 5S RRNA E-LOOP/L25 COMPLEX
Keywords keywordsPROTEIN-RNA COMPLEX, RIBOSOME; RIBOSOME
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.14
Radius of gyration Rg (electron density) rg_electron18.68
Forward intensity I(0) i05570540000.00
Molecular weight molecular_weight454820.0 kDa
Excluded volume excluded_volume494640 ų
Envelope volume envelope_volume51204 ų
Hydration-shell volume shell_volume20515 ų
Envelope diameter envelope_diameter80.8
Shell Rg shell_rg28.01
Envelope Rg envelope_rg22.60
Shape Rg shape_rg18.57
Total Rg total_rg19.00
Total atoms total_atoms54580
Residues n_residues2620
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 dmax71.2
Rg (real space) rg_real19.27
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real5.5710e+09
I(0) uncertainty (real space) i0_real_error8.1800e+07
Rg (reciprocal space) rg_reciprocal19.25
I(0) (reciprocal space) i0_reciprocal5570000000.0000
Solution quality estimate total_estimate0.7344
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.8
Skewness Skewness skewness0.521
Kurtosis Kurtosis kurtosis-0.081
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1654000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.651; Stabil: 0.993; Sysdev: 1.000; Positv: 1.000; Valcen: 0.610; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1d6ka_
Class classb — All beta proteins
Fold Fold foldb.53 — Ribosomal protein L25-like
Superfamily Superfamily superfamilyb.53.1 — Ribosomal protein L25-like
Family Family familyb.53.1.1 — Ribosomal protein L25-like

CATH v4.4 (1 domains)

Domain ID domain_id1d6kA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology240 — Ribosomal Protein L25; Chain P
Homologous superfamily homologous superfamily10 — Ribosomal Protein L25; Chain P

8. Citations (1)

9. Files and Curves (10)