2aas

HIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE A IN SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

Method: SOLUTION NMR Dmax: 41.8 Å Quality: EXCELLENT

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

RIBONUCLEASE A

Bos taurus

UniProt P61823

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 27–150 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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.

333 other PDB entries and 495 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNAS1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–124; UniProt 27–150

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 2aas

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2aas
Deposition date deposition_date1992-11-20
Structure title titleHIGH-RESOLUTION THREE-DIMENSIONAL STRUCTURE OF RIBONUCLEASE A IN SOLUTION BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
Keywords keywordsHYDROLASE(ENDORIBONUCLEASE); HYDROLASE(ENDORIBONUCLEASE)
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.17
Radius of gyration Rg (electron density) rg_electron14.24
Forward intensity I(0) i03195200000.00
Molecular weight molecular_weight438220.0 kDa
Excluded volume excluded_volume530800 ų
Envelope volume envelope_volume26403 ų
Hydration-shell volume shell_volume14357 ų
Envelope diameter envelope_diameter53.2
Shell Rg shell_rg21.36
Envelope Rg envelope_rg15.90
Shape Rg shape_rg14.23
Total Rg total_rg14.30
Total atoms total_atoms38272
Residues n_residues3968
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 dmax41.8
Rg (real space) rg_real14.12
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real3.1950e+09
I(0) uncertainty (real space) i0_real_error2.9960e+07
Rg (reciprocal space) rg_reciprocal14.13
I(0) (reciprocal space) i0_reciprocal3195000000.0000
Solution quality estimate total_estimate0.9175
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.3
Skewness Skewness skewness0.203
Kurtosis Kurtosis kurtosis-0.534
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha330700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.986; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.966

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_idd2aasa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.5 — RNase A-like
Superfamily Superfamily superfamilyd.5.1 — RNase A-like
Family Family familyd.5.1.1 — Ribonuclease A-like

CATH v4.4 (1 domains)

Domain ID domain_id2aasA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain

8. Citations (5)

9. Files and Curves (10)