1c04

IDENTIFICATION OF KNOWN PROTEIN AND RNA STRUCTURES IN A 5 A MAP OF THE LARGE RIBOSOMAL SUBUNIT FROM HALOARCULA MARISMORTUI

Method: X-RAY DIFFRACTION Dmax: 119.0 Å Quality: REASONABLE

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

RIBOSOMAL PROTEIN L2

OrganismNot specified

UniProt P04257

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 Heteromer Protein × 4 RNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 60–196 Fragment:CENTRAL RNA-BINDING DOMAINS Non-standard monomer:Yes (specific site not provided by mmCIF) 23S RRNA FRAGMENT × 1 23S RRNA FRAGMENT × 1 RIBOSOMAL PROTEIN L6 × 1 (P02391) RIBOSOMAL PROTEIN L11 × 1 (P56210) RIBOSOMAL PROTEIN L14 × 1 (P04450) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.4;292 K;PEG 6000, POTASSIUM CHLORIDE, AMMONIUM CHLORIDE, MAGNESIUM CHLORIDE, ACETATE, pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 5.00 Å

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.

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

View Construct and Data Evidence
UniProt name RL2_BACST
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–137; UniProt 60–196

RIBOSOMAL PROTEIN L6

OrganismNot specified

UniProt P02391

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 Heteromer Protein × 4 RNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain B; UniProt 1–177 Not recorded 23S RRNA FRAGMENT × 1 23S RRNA FRAGMENT × 1 RIBOSOMAL PROTEIN L2 × 1 (P04257) RIBOSOMAL PROTEIN L11 × 1 (P56210) RIBOSOMAL PROTEIN L14 × 1 (P04450) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.4;292 K;PEG 6000, POTASSIUM CHLORIDE, AMMONIUM CHLORIDE, MAGNESIUM CHLORIDE, ACETATE, pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 5.00 Å

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.

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

View Construct and Data Evidence
UniProt name RL6_BACST
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–177; UniProt 1–177

RIBOSOMAL PROTEIN L11

OrganismNot specified

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–RNA Heteromer Protein × 4 RNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain C; UniProt 63–129 Fragment:C-TERMINAL DOMAIN 23S RRNA FRAGMENT × 1 23S RRNA FRAGMENT × 1 RIBOSOMAL PROTEIN L2 × 1 (P04257) RIBOSOMAL PROTEIN L6 × 1 (P02391) RIBOSOMAL PROTEIN L14 × 1 (P04450) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.4;292 K;PEG 6000, POTASSIUM CHLORIDE, AMMONIUM CHLORIDE, MAGNESIUM CHLORIDE, ACETATE, pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 5.00 Å

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 5
Chains and sequence ranges Author chain C; PDBConstruct 1–67; UniProt 63–129

RIBOSOMAL PROTEIN L14

OrganismNot specified

UniProt P04450

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 Heteromer Protein × 4 RNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain D; UniProt 1–122 Not recorded 23S RRNA FRAGMENT × 1 23S RRNA FRAGMENT × 1 RIBOSOMAL PROTEIN L2 × 1 (P04257) RIBOSOMAL PROTEIN L6 × 1 (P02391) RIBOSOMAL PROTEIN L11 × 1 (P56210) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.4;292 K;PEG 6000, POTASSIUM CHLORIDE, AMMONIUM CHLORIDE, MAGNESIUM CHLORIDE, ACETATE, pH 5.4, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 5.00 Å

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL14_BACST
Isoform
PDB entities 6
Chains and sequence ranges Author chain D; PDBConstruct 1–122; UniProt 1–122

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 1c04

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c04
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c04
Deposition date deposition_date1999-07-14
Structure title titleIDENTIFICATION OF KNOWN PROTEIN AND RNA STRUCTURES IN A 5 A MAP OF THE LARGE RIBOSOMAL SUBUNIT FROM HALOARCULA MARISMORTUI
Keywords keywordsLOW RESOLUTION MODEL, LARGE RIBOSOME UNIT, RIBOSOME; RIBOSOME
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier58.51
Radius of gyration Rg (electron density) rg_electron64.80
Forward intensity I(0) i0153885000.00
Molecular weight molecular_weight81179.0 kDa
Excluded volume excluded_volume92874 ų
Envelope volume envelope_volume198120 ų
Hydration-shell volume shell_volume30972 ų
Envelope diameter envelope_diameter202.3
Shell Rg shell_rg52.11
Envelope Rg envelope_rg62.69
Shape Rg shape_rg64.80
Total Rg total_rg64.38
Total atoms total_atoms5570
Residues n_residues572
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 dmax119.0
Rg (real space) rg_real42.39
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real1.3040e+08
I(0) uncertainty (real space) i0_real_error2.0980e+06
Rg (reciprocal space) rg_reciprocal56.82
I(0) (reciprocal space) i0_reciprocal153000000.0000
Solution quality estimate total_estimate0.5749
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary30.8
Skewness Skewness skewness0.229
Kurtosis Kurtosis kurtosis-0.924
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha1.2640
Highest regularization parameter α highest_alpha1450000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.020; Oscil: 0.972; Stabil: 0.966; Sysdev: 0.000; Positv: 1.000; Valcen: 0.659; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1c04a_
Class classi — Low resolution protein structures
Fold Fold foldi.1 — Ribosome and ribosomal fragments
Superfamily Superfamily superfamilyi.1.1 — Ribosome and ribosomal fragments
Family Family familyi.1.1.2 — Large subunit
Domain ID domain_idd1c04b_
Class classi — Low resolution protein structures
Fold Fold foldi.1 — Ribosome and ribosomal fragments
Superfamily Superfamily superfamilyi.1.1 — Ribosome and ribosomal fragments
Family Family familyi.1.1.2 — Large subunit
Domain ID domain_idd1c04c_
Class classi — Low resolution protein structures
Fold Fold foldi.1 — Ribosome and ribosomal fragments
Superfamily Superfamily superfamilyi.1.1 — Ribosome and ribosomal fragments
Family Family familyi.1.1.2 — Large subunit
Domain ID domain_idd1c04d_
Class classi — Low resolution protein structures
Fold Fold foldi.1 — Ribosome and ribosomal fragments
Superfamily Superfamily superfamilyi.1.1 — Ribosome and ribosomal fragments
Family Family familyi.1.1.2 — Large subunit

8. Citations (2)

9. Files and Curves (10)