2cql

Solution structure of the N-terminal domain of human ribosomal protein L9

Method: SOLUTION NMR Dmax: 42.0 Å Quality: REASONABLE

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

60S ribosomal protein L9

Homo sapiens

UniProt P32969

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 1–87 Fragment:N-terminal domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 120mM;Pressure ambient NMR sample composition:1.4mM 13C/15N-PROTEIN; 20mM d-Tris-HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3 | 90% H2O/10% 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.

172 other PDB entries and 172 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RL9_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–94; UniProt 1–87

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 2cql

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2cql
Deposition date deposition_date2005-05-20
Structure title titleSolution structure of the N-terminal domain of human ribosomal protein L9
Keywords keywords;N-terminal domain, alpha and beta (a+b), Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, TRANSLATION ;; TRANSLATION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.59
Radius of gyration Rg (electron density) rg_electron15.13
Forward intensity I(0) i0687411000.00
Molecular weight molecular_weight218420.0 kDa
Excluded volume excluded_volume273670 ų
Envelope volume envelope_volume37120 ų
Hydration-shell volume shell_volume16677 ų
Envelope diameter envelope_diameter70.8
Shell Rg shell_rg25.27
Envelope Rg envelope_rg20.49
Shape Rg shape_rg15.09
Total Rg total_rg15.49
Total atoms total_atoms31520
Residues n_residues2000
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 dmax42.0
Rg (real space) rg_real14.72
Rg uncertainty (real space) rg_real_error0.07
I(0) (real space) i0_real6.5600e+08
I(0) uncertainty (real space) i0_real_error6.3020e+06
Rg (reciprocal space) rg_reciprocal15.70
I(0) (reciprocal space) i0_reciprocal687400000.0000
Solution quality estimate total_estimate0.6803
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.324
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha4.0220
Highest regularization parameter α highest_alpha176100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.002; Oscil: 0.969; Stabil: 0.979; Sysdev: 0.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2cqla1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.141 — Ribosomal protein L6
Superfamily Superfamily superfamilyd.141.1 — Ribosomal protein L6
Family Family familyd.141.1.1 — Ribosomal protein L6
Domain ID domain_idd2cqla2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2cqla3
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_id2cqlA01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology930 — Outer Surface Protein A; domain 3
Homologous superfamily homologous superfamily12 — Ribosomal protein L6

8. Citations (1)

9. Files and Curves (10)