3i67

Ribonuclease A by LB nanotemplate method after high X-Ray dose on ESRF ID14-2 beamline

Method: X-RAY DIFFRACTION Dmax: 50.9 Å Quality: GOOD

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

Ribonuclease pancreatic

OrganismNot specified

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 27–150 Not recorded CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;1.75M ammonium sulphate, 2.0M Sodium Chloride, 100mM Na-acetate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 1.30 Å R-free 0.237

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 3i67

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3i67
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3i67
Deposition date deposition_date2009-07-06
Structure title titleRibonuclease A by LB nanotemplate method after high X-Ray dose on ESRF ID14-2 beamline
Keywords keywordsRibonuclease A, Disulfide bond, Endonuclease, Glycation, Glycoprotein, Hydrolase, Nuclease, Secreted; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.31
Radius of gyration Rg (electron density) rg_electron14.38
Forward intensity I(0) i04466420.00
Molecular weight molecular_weight13730.0 kDa
Excluded volume excluded_volume16610 ų
Envelope volume envelope_volume19267 ų
Hydration-shell volume shell_volume11619 ų
Envelope diameter envelope_diameter50.2
Shell Rg shell_rg19.72
Envelope Rg envelope_rg14.72
Shape Rg shape_rg14.39
Total Rg total_rg15.38
Total atoms total_atoms952
Residues n_residues124
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 dmax50.9
Rg (real space) rg_real15.26
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real4.4660e+06
I(0) uncertainty (real space) i0_real_error5.1460e+04
Rg (reciprocal space) rg_reciprocal15.26
I(0) (reciprocal space) i0_reciprocal4466000.0000
Solution quality estimate total_estimate0.8869
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.4
Skewness Skewness skewness0.248
Kurtosis Kurtosis kurtosis-0.397
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha954400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.965

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3i67a_
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_id3i67A00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain

8. Citations (1)

9. Files and Curves (10)