1c54

SOLUTION STRUCTURE OF RIBONUCLEASE SA

Method: SOLUTION NMR Dmax: 67.8 Å Quality: GOOD

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

RIBONUCLEASE SA

Streptomyces aureofaciens

UniProt P05798

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 1–96 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5.5;303.2 K;Ionic strength (raw mmCIF value) 0;Pressure AMBIENT NMR measurement conditions:pH 5.5;303.2 K;Ionic strength (raw mmCIF value) 0;Pressure AMBIENT NMR measurement conditions:pH 5.5;303.2 K;Ionic strength (raw mmCIF value) 0;Pressure AMBIENT NMR measurement conditions:pH 5.5;303.2 K;Ionic strength (raw mmCIF value) 0;Pressure AMBIENT NMR sample composition:NA NMR sample composition:NA NMR sample composition:U-15N NMR sample composition:U-15N 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.

27 other PDB entries and 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNSA_STRAU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–96; UniProt 1–96

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 1c54

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c54
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c54
Deposition date deposition_date1999-10-22
Structure title titleSOLUTION STRUCTURE OF RIBONUCLEASE SA
Keywords keywordsALPHA+BETA PROTEIN, HYDROLASE; HYDROLASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier17.53
Radius of gyration Rg (electron density) rg_electron17.03
Forward intensity I(0) i0682258000.00
Molecular weight molecular_weight211370.0 kDa
Excluded volume excluded_volume260650 ų
Envelope volume envelope_volume79053 ų
Hydration-shell volume shell_volume29165 ų
Envelope diameter envelope_diameter72.0
Shell Rg shell_rg29.83
Envelope Rg envelope_rg21.88
Shape Rg shape_rg17.01
Total Rg total_rg17.52
Total atoms total_atoms18180
Residues n_residues1920
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 dmax67.8
Rg (real space) rg_real17.52
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real6.8230e+08
I(0) uncertainty (real space) i0_real_error1.0090e+07
Rg (reciprocal space) rg_reciprocal17.52
I(0) (reciprocal space) i0_reciprocal682300000.0000
Solution quality estimate total_estimate0.7824
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.8
Skewness Skewness skewness0.440
Kurtosis Kurtosis kurtosis-0.006
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha61380000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.465; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.775; Smooth: 0.998

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_idd1c54a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.1 — Microbial ribonucleases
Superfamily Superfamily superfamilyd.1.1 — Microbial ribonucleases
Family Family familyd.1.1.2 — Bacterial ribonucleases

CATH v4.4 (1 domains)

Domain ID domain_id1c54A00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology450 — Nuclear Transport Factor 2; Chain: A,
Homologous superfamily homologous superfamily30 — Microbial ribonucleases

8. Citations (3)

9. Files and Curves (10)