2fow

THE RNA BINDING DOMAIN OF RIBOSOMAL PROTEIN L11: THREE-DIMENSIONAL STRUCTURE OF THE RNA-BOUND FORM OF THE PROTEIN, NMR, 26 STRUCTURES

Method: SOLUTION NMR Dmax: 32.8 Å Quality: REASONABLE

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

RIBOSOMAL PROTEIN L11

Geobacillus stearothermophilus

UniProt P56210

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 59–133 Fragment:C-TERMINAL DOMAIN, 75 RESIDUES Mutation:F1M No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.1;320 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.

8 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL11_BACST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–76; UniProt 59–133

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 2fow

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2fow
Deposition date deposition_date1997-05-26
Structure title titleTHE RNA BINDING DOMAIN OF RIBOSOMAL PROTEIN L11: THREE-DIMENSIONAL STRUCTURE OF THE RNA-BOUND FORM OF THE PROTEIN, NMR, 26 STRUCTURES
Keywords keywordsRIBOSOME, PROTEIN:RNA, THIOSTREPTON; RIBOSOME
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.01
Radius of gyration Rg (electron density) rg_electron12.73
Forward intensity I(0) i0632394000.00
Molecular weight molecular_weight211710.0 kDa
Excluded volume excluded_volume265850 ų
Envelope volume envelope_volume29465 ų
Hydration-shell volume shell_volume15010 ų
Envelope diameter envelope_diameter57.9
Shell Rg shell_rg22.59
Envelope Rg envelope_rg17.36
Shape Rg shape_rg12.72
Total Rg total_rg13.01
Total atoms total_atoms30394
Residues n_residues1976
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 dmax32.8
Rg (real space) rg_real12.42
Rg uncertainty (real space) rg_real_error0.04
I(0) (real space) i0_real6.0550e+08
I(0) uncertainty (real space) i0_real_error4.4880e+06
Rg (reciprocal space) rg_reciprocal13.03
I(0) (reciprocal space) i0_reciprocal632400000.0000
Solution quality estimate total_estimate0.6878
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary15.0
Skewness Skewness skewness0.183
Kurtosis Kurtosis kurtosis-0.545
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha3.6930
Highest regularization parameter α highest_alpha155400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.998; Stabil: 0.983; Sysdev: 0.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2fowa_
Class classa — All alpha proteins
Fold Fold folda.4 — DNA/RNA-binding 3-helical bundle
Superfamily Superfamily superfamilya.4.7 — Ribosomal protein L11, C-terminal domain
Family Family familya.4.7.1 — Ribosomal protein L11, C-terminal domain

CATH v4.4 (1 domains)

Domain ID domain_id2fowA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily250 — Ribosomal protein L11/L12, C-terminal domain

8. Citations (1)

9. Files and Curves (10)